A cystatin subtype that has a diverse tissue distribution, target specificity, and functions as an endogenous inhibitor of lysosomal cysteine proteases.
A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.
An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.
A chronic, congenital ichthyosis inherited as an autosomal recessive trait. Infants are usually born encased in a collodion membrane which sheds within a few weeks. Scaling is generalized and marked with grayish-brown quadrilateral scales, adherent at their centers and free at the edges. In some cases, scales are so thick that they resemble armored plate.
An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.
A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
The external, nonvascular layer of the skin. It is made up, from within outward, of five layers of EPITHELIUM: (1) basal layer (stratum basale epidermidis); (2) spinous layer (stratum spinosum epidermidis); (3) granular layer (stratum granulosum epidermidis); (4) clear layer (stratum lucidum epidermidis); and (5) horny layer (stratum corneum epidermidis).
Sweat-producing structures that are embedded in the DERMIS. Each gland consists of a single tube, a coiled body, and a superficial duct.
Any of several generalized skin disorders characterized by dryness, roughness, and scaliness, due to hypertrophy of the stratum corneum epidermis. Most are genetic, but some are acquired, developing in association with other systemic disease or genetic syndrome.
A tube-like invagination of the EPIDERMIS from which the hair shaft develops and into which SEBACEOUS GLANDS open. The hair follicle is lined by a cellular inner and outer root sheath of epidermal origin and is invested with a fibrous sheath derived from the dermis. (Stedman, 26th ed) Follicles of very long hairs extend into the subcutaneous layer of tissue under the SKIN.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
A group of closely-related cystatins found in SALIVA.
Transglutaminases catalyze cross-linking of proteins at a GLUTAMINE in one chain with LYSINE in another chain. They include keratinocyte transglutaminase (TGM1 or TGK), tissue transglutaminase (TGM2 or TGC), plasma transglutaminase involved with coagulation (FACTOR XIII and FACTOR XIIIa), hair follicle transglutaminase, and prostate transglutaminase. Although structures differ, they share an active site (YGQCW) and strict CALCIUM dependence.
The functions of the skin in the human and animal body. It includes the pigmentation of the skin.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Endogenous peptides present in most body fluids. Certain enzymes convert them to active KININS which are involved in inflammation, blood clotting, complement reactions, etc. Kininogens belong to the cystatin superfamily. They are cysteine proteinase inhibitors. HIGH-MOLECULAR-WEIGHT KININOGEN; (HMWK); is split by plasma kallikrein to produce BRADYKININ. LOW-MOLECULAR-WEIGHT KININOGEN; (LMWK); is split by tissue kallikrein to produce KALLIDIN.
A single-pass type I membrane protein. It is cleaved by AMYLOID PRECURSOR PROTEIN SECRETASES to produce peptides of varying amino acid lengths. A 39-42 amino acid peptide, AMYLOID BETA-PEPTIDES is a principal component of the extracellular amyloid in SENILE PLAQUES.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
A degenerative disease of the BRAIN characterized by the insidious onset of DEMENTIA. Impairment of MEMORY, judgment, attention span, and problem solving skills are followed by severe APRAXIAS and a global loss of cognitive abilities. The condition primarily occurs after age 60, and is marked pathologically by severe cortical atrophy and the triad of SENILE PLAQUES; NEUROFIBRILLARY TANGLES; and NEUROPIL THREADS. (From Adams et al., Principles of Neurology, 6th ed, pp1049-57)
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.

Cystatin M/E expression is restricted to differentiated epidermal keratinocytes and sweat glands: a new skin-specific proteinase inhibitor that is a target for cross-linking by transglutaminase. (1/27)

Using serial analysis of gene expression on cultured human keratinocytes we found high expression levels of genes putatively involved in host protection and defense, such as proteinase inhibitors and antimicrobial proteins. One of these expressed genes was the recently discovered cysteine proteinase inhibitor cystatin M/E that has not been characterized so far at the protein level with respect to tissue distribution and additional biologic properties. Here we report that cystatin M/E has a tissue-specific expression pattern in which high expression levels are restricted to the stratum granulosum of normal human skin, the stratum granulosum/spinosum of psoriatic skin, and the secretory coils of eccrine sweat glands. Low expression levels were found in the nasal cavity. The presence of cystatin M/E in skin and the lack of expression in a variety of other tissues was verified both at the protein level by immunohistochemistry or western blotting, and at the mRNA level by reverse transcriptase polymerase chain reaction or northern blotting. Using biotinylated hexapeptide probes we found that cystatin M/E is an efficient substrate for tissue type transglutaminase and for transglutaminases extracted from stratum corneum, and that it acts as an acyl acceptor but not as an acyl donor. Western blot analysis showed that recombinant cystatin M/E could be cross-linked to a variety of proteins extracted from stratum corneum. In vitro, we found that cystatin M/E expression in cultured keratinocytes is upregulated at the mRNA and protein level, upon induction of differentiation. We demonstrate that cystatin M/E, which has a putative signal peptide, is indeed a secreted protein and is found in vitro in culture supernatant and in vivo in human sweat by enzyme-linked immunosorbent assay or western blotting. Cystatin M/E showed moderate inhibition of cathepsin B but was not active against cathepsin C. We speculate that cystatin M/E is unlikely to be a physiologically relevant inhibitor of intracellular lysosomal cysteine proteinases but rather functions as an inhibitor of self and nonself cysteine proteinases that remain to be identified.  (+info)

A null mutation in the cystatin M/E gene of ichq mice causes juvenile lethality and defects in epidermal cornification. (2/27)

Cystatin M/E (CST6 ), a new member of the cystatin gene family, has a restricted expression pattern in humans, which is largely limited to cutaneous epithelia. Although cystatin M/E possesses two distinct biochemical properties, being a cysteine proteinase inhibitor and a substrate for transglutaminase, its physiological function is unknown. Here we report the isolation and characterization of the mouse Cst6 orthologue and the assignment of the chromosomal localization to the proximal end of mouse chromosome 19. This region corresponds to the locus of the spontaneous harlequin ichthyosis (ichq) mouse mutation, for which no causative gene has been identified so far. We found a nonsense mutation in the Cst6 gene of BALB/cJ-ichq/+ mice, which precludes the synthesis of functional protein. Immunohistochemistry confirmed the absence of cystatin M/E at the protein level in ichq/ichq mice. Mice that are homozygous for two null alleles display a hyperplastic, hyperkeratotic epidermis and abnormal hair follicles, and die between 5 and 12 days of age. In wild-type mice, cystatin M/E was found in the stratum granulosum and in the infundibulum of the hair follicle indicating that the anatomical site in the skin where cystatin M/E is normally expressed correlates with the abnormalities at the tissue level in ichq/ichq mice. Our data provide evidence that cystatin M/E is required for viability and for correct formation of cornified layers in the epidermis and hair follicles. The ichq mouse mutation may serve as a model for human type 2 harlequin ichthyosis.  (+info)

Cystatin E1 and E2, new members of male reproductive tract subgroup within cystatin type 2 family. (3/27)

The family of type 2 cystatin proteins is a class of cysteine proteinase inhibitors that function as potent inhibitors of papain-like cysteine proteinases. Recent studies have suggested that cystatins in the male reproductive tract subgroup may perform functions distinct from those of typical cystatins. The objective of the present study was to identify and characterize the expression of new gene members of the cystatin family 2 in mouse male reproductive tissues. Two new members of cystatin family 2, named mouse Cystatin E1 and mouse Cystatin E2 (mCST E1 and mCST E2, respectively), were identified in mice by searching the National Center for Biotechnology Information database for proteins containing homology to known type 2 cystatins. Human CST E1 has recently been reported independently under the name CST 11. The deduced amino acid sequences of these genes have significant homology with the family 2 cystatins, including four conserved cysteine residues at the C-terminus. Similar to other male reproductive subgroup cystatins, the inhibitory motifs are not well conserved in these genes. Northern blot analyses showed that both genes were highly expressed only in the epididymis. In situ hybridization demonstrated that both genes were restricted in their expression to the epithelial cells of the caput and that the highest expression was localized to the initial segment of caput epididymis. Northern blot analyses and in situ hybridization showed that both mCST E1 and E2 mRNA decreased after castration, and treatment with testosterone propionate (T) did not maintain expression of these genes. In fact, T treatment further repressed the expression of these genes in the epididymis following castration. Efferent ductule ligation resulted in a dramatic decrease of epididymal expression of mCST E1 and E2. The expression of mCST E1 mRNA was up-regulated by 17 beta-estradiol (E) administration for 7 days postcastration, whereas no recovery of mCST E1 mRNA level was detected after 14 days of E treatment. Combined E and T (E+T) treatment for 1 and 2 wk reduced the mCST E1 transcripts. The expression of mCST E2 mRNA was maintained by E administration for both 7 and 14 days after castration, whereas treatment of both T and E repressed the expression of mCST E2. Although both mCST E1 and E2 share significant homology with family 2 cystatins, including similar distribution in tissues and localization in epididymis, these genes may have different functions, because their regulation involves different hormones and, probably, other testicular factors.  (+info)

The human cystatin M/E gene (CST6): exclusion candidate gene for harlequin ichthyosis. (4/27)

Cystatin M/E is a recently discovered cysteine proteinase inhibitor whose expression is largely confined to cutaneous epithelia. In human skin it is expressed in sweat glands, hair follicles, and stratum granulosum of the epidermis where it presumably acts as a substrate for transglutaminase. Very recently we reported that a null mutation in the mouse cystatin M/E gene (Cst6) causes the murine ichq phenotype, which is characterized by abnormalities in cornification and desquamation, demonstrating an essential role for cystatin M/E in the final stages of epidermal differentiation. We here obtained the complete sequence of the human cystatin M/E gene (CST6), which provides a tool to investigate CST6 as a candidate gene in skin diseases characterized by abnormal cornification. The involvement of CST6 in harlequin ichthyosis in humans was evaluated by sequencing the entire coding region and intron-exon boundaries for mutations in 11 sporadic harlequin ichthyosis patients. No CST6 mutations were detected in this group, which comprised type 1 and type 2 harlequin ichthyosis patients. Disturbed transcription/translation due to mutations in regulatory and noncoding regions of cystatin M/E was unlikely because cystatin M/E protein expression was observed in all patients examined, as assessed by immunohistochemistry. Although our results indicate that CST6 is not a major gene contributing to type 1 and 2 harlequin ichthyosis, these data may facilitate further analysis of the role of cystatin M/E in normal human skin and other genetic disorders of cornification.  (+info)

Evidence that unrestricted legumain activity is involved in disturbed epidermal cornification in cystatin M/E deficient mice. (5/27)

Homozygosity for Cst6 null alleles causes the phenotype of the ichq mouse, which is a model for human harlequin ichthyosis (OMIM 242500), a genetically heterogeneous group of keratinization disorders. Here we report evidence for the mechanism by which deficiency of the cysteine protease inhibitor cystatin M/E (the Cst6 gene product) leads to disturbed cornification, impaired barrier function and dehydration. Absence of cystatin M/E causes unrestricted activity of its target protease legumain in hair follicles and epidermis, which is the exact location where cystatin M/E is normally expressed. Analysis of stratum corneum proteins revealed a strong decrease of soluble loricrin monomers in skin extracts of ichq mice, although normal levels of loricrin were present in the stratum granulosum and stratum corneum of ichq mice, as shown by immunohistochemistry. This suggested a premature or enhanced crosslinking of loricrin monomers in ichq mice by transglutaminase 3 (TGase 3). In these mice, we indeed found strongly increased levels of TGase 3 that was processed into its activated 30 and 47 kDa subunits, compared to wild-type mice. This study shows that cystatin M/E and legumain form a functional dyad in epidermis in vivo. Disturbance of this protease-antiprotease balance causes increased enzyme activity of TGase 3 that could explain the observed abnormal cornification.  (+info)

Cystatin m: a novel candidate tumor suppressor gene for breast cancer. (6/27)

The contribution of pericellular proteolysis to tumor progression is well documented. To better understand protease biology and facilitate clinical translation, specific proteolytic systems need to be better defined. In particular, the precise role of endogenous protease inhibitors still needs to be deciphered. We reported previously that cystatin M, a potent endogenous inhibitor of lysosomal cysteine proteases, significantly suppressed in vitro cell proliferation, migration, and Matrigel invasion. Here, we show that scid mice orthotopically implanted with breast cancer cells expressing cystatin M show significantly delayed primary tumor growth and lower metastatic burden in the lungs and liver when compared with mice implanted with mock controls. The incidence of metastasis, however, appeared to be unaltered between the cystatin M group and the control group. Experimental metastasis assays suggest that cystatin M suppressed tumor cell proliferation at the secondary site. By using laser capture microdissection and quantitative reverse transcription-polymerase chain reaction, we found consistent expression of cystatin M in normal human breast epithelial cells, whereas expression was decreased by 86% in invasive ductal carcinoma (IDC) cells of stage I to IV patients. Complete loss of expression of cystatin M was observed in two of three IDCs from stage IV patients. Immunohistochemical studies confirmed that expression of cystatin M in IDCs was partially or completely lost. We propose cystatin M as a novel candidate tumor suppressor gene for breast cancer.  (+info)

Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification. (7/27)

Cystatin M/E is a high affinity inhibitor of the asparaginyl endopeptidase legumain, and we have previously reported that both proteins are likely to be involved in the regulation of stratum corneum formation in skin. Although cystatin M/E contains a predicted binding site for papain-like cysteine proteases, no high affinity binding for any member of this family has been demonstrated so far. We report that human cathepsin V (CTSV) and human cathepsin L (CTSL) are strongly inhibited by human cystatin M/E. Kinetic studies show that Ki values of cystatin M/E for the interaction with CTSV and CTSL are 0.47 and 1.78 nM, respectively. On the basis of the analogous sites in cystatin C, we used site-directed mutagenesis to identify the binding sites of these proteases in cystatin M/E. We found that the W135A mutant was rendered inactive against CTSV and CTSL but retained legumain-inhibiting activity. Conversely, the N64A mutant lost legumain-inhibiting activity but remained active against the papain-like cysteine proteases. We conclude that legumain and papain-like cysteine proteases are inhibited by two distinct non-overlapping sites. Using immunohistochemistry on normal human skin, we found that cystatin M/E co-localizes with CTSV and CTSL. In addition, we show that CTSL is the elusive enzyme that processes and activates epidermal transglutaminase 3. The identification of CTSV and CTSL as novel targets for cystatin M/E, their (co)-expression in the stratum granulosum of human skin, and the activity of CTSL toward transglutaminase 3 strongly imply an important role for these enzymes in the differentiation process of human epidermis.  (+info)

Colocalization of cystatin M/E and cathepsin V in lamellar granules and corneodesmosomes suggests a functional role in epidermal differentiation. (8/27)

Cystatin M/E is a cysteine protease inhibitor with two distinct binding sites for papain-like cysteine proteases (family C1) and the asparaginyl endopeptidase (AEP) legumain of family C13. We have previously demonstrated that deficiency of cystatin M/E in mice causes ichthyosiform skin changes and barrier disruption, which could be caused by unrestrained AEP activity. Recently, we provided biochemical evidence that human cathepsin V (CTSV) and cathepsin L (CTSL) are additional biological targets for human cystatin M/E. To address the possible role of these three proteases and their inhibitor in epidermal differentiation, we investigated the localization of these proteins in normal human skin. Whereas CTSL and AEP were broadly expressed in epithelial cells of the skin, we found a specific colocalization of cystatin M/E and CTSV in the stratum granulosum and in the root sheets of the hair follicle, using immunofluorescence microscopy. Immunoelectron microscopy revealed that cystatin M/E and CTSV are separately transported within the lamellar granules. Cystatin M/E was also found in the extracellular space in the stratum corneum associated with corneodesmosomes, where it was closely associated with CTSV. Based on the striking stratum-specific colocalization of cystatin M/E and CTSV, we propose that these molecules could have an important role in epidermal differentiation and desquamation.  (+info)

Cystatin M is a type of cysteine protease inhibitor that is primarily expressed in the epididymis, a tube-like structure in the male reproductive system where sperm maturation occurs. It belongs to the cystatin superfamily, which are proteins that regulate protein catabolism by inhibiting the activity of cysteine proteases.

Cystatin M is encoded by the CST6 gene and has been shown to play a role in sperm maturation and fertility. It is secreted into the lumen of the epididymis, where it interacts with sperm and other proteins to regulate their function. Mutations in the CST6 gene have been associated with male infertility, suggesting that cystatin M plays an important role in reproductive health.

In addition to its role in the male reproductive system, cystatin M has also been found in other tissues and may have additional functions beyond regulating cysteine proteases. However, further research is needed to fully understand the physiological roles of this protein.

Cystatins are a group of proteins that inhibit cysteine proteases, which are enzymes that break down other proteins. Cystatins are found in various biological fluids and tissues, including tears, saliva, seminal plasma, and urine. They play an important role in regulating protein catabolism and protecting cells from excessive protease activity. There are three main types of cystatins: type 1 (cystatin C), type 2 (cystatin M, cystatin N, and fetuin), and type 3 (kininogens). Abnormal levels of cystatins have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Cystatin C is a protein produced by many cells in the body, including all types of nucleated cells. It is a member of the cysteine protease inhibitor family and functions as an endogenous inhibitor of cathepsins, which are proteases involved in various physiological and pathological processes such as extracellular matrix degradation, antigen presentation, and cell death.

Cystatin C is freely filtered by the glomeruli in the kidneys and almost completely reabsorbed and catabolized by the proximal tubules. Therefore, its serum concentration is a reliable marker of glomerular filtration rate (GFR) and can be used to estimate kidney function.

Increased levels of cystatin C in the blood may indicate impaired kidney function or kidney disease, while decreased levels are less common and may be associated with hyperfiltration or overproduction of cystatin C. Measuring cystatin C levels can complement or supplement traditional methods for assessing kidney function, such as estimating GFR based on serum creatinine levels.

Lamellar Ichthyosis is a rare, inherited genetic skin disorder characterized by widespread, persistent scaling of the skin. It is caused by mutations in genes responsible for maintaining the barrier function and hydration of the skin. The condition is present from birth and can vary in severity.

In lamellar ichthyosis, the skin cells do not shed properly and instead accumulate in plates or scales that cover the entire body. These scales are large, dark brown or gray, and have a cracked appearance, resembling fish scales. The scales may be present at birth (congenital) or develop within the first few weeks of life.

The skin is also prone to redness, irritation, and infection due to the impaired barrier function. Other symptoms can include overheating, dehydration, and difficulty with sweating. The condition may improve in warmer, more humid environments.

Treatment for lamellar ichthyosis is aimed at managing symptoms and preventing complications. This may include topical creams and ointments to moisturize the skin, medications to reduce inflammation and infection, and avoiding environmental triggers that can worsen symptoms. In some cases, oral retinoids may be prescribed to help regulate skin cell growth and shedding.

Cystatin B is a type of protease inhibitor that belongs to the cystatin superfamily. It is primarily produced in the central nervous system and is found in various body fluids, including cerebrospinal fluid and urine. Cystatin B plays a crucial role in regulating protein catabolism by inhibiting lysosomal cysteine proteases, which are enzymes that break down proteins.

Defects or mutations in the gene that encodes for cystatin B have been associated with a rare inherited neurodegenerative disorder known as Uner Tan Syndrome (UTS). UTS is characterized by language impairment, mental retardation, and distinctive facial features. The exact mechanism by which cystatin B deficiency leads to this disorder is not fully understood, but it is thought to involve the dysregulation of protein catabolism in neurons, leading to neurotoxicity and neurodegeneration.

Cystatin A is a type of cysteine protease inhibitor that is primarily produced by cells of the immune system. It is a small protein consisting of 120 amino acids and is encoded by the CSTA gene in humans. Cystatin A functions to regulate the activity of cathepsins, which are enzymes that break down proteins in the body.

Cystatin A is mainly found inside cells, where it helps to maintain the balance of cathepsins and prevent excessive protein degradation. However, it can also be released into extracellular spaces under certain conditions, such as inflammation or cell damage. In the extracellular space, cystatin A may help to regulate the activity of cathepsins in the surrounding tissue and contribute to the regulation of immune responses.

Abnormal levels of cystatin A have been associated with various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. However, more research is needed to fully understand the role of cystatin A in these conditions and its potential as a therapeutic target.

Cathepsin L is a lysosomal cysteine protease that plays a role in various physiological processes, including protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor and activated by cleavage of its propeptide domain. Cathepsin L has a broad specificity for peptide bonds and can cleave both intracellular and extracellular proteins, making it an important player in various pathological conditions such as cancer, neurodegenerative diseases, and infectious diseases. Inhibition of cathepsin L has been explored as a potential therapeutic strategy for these conditions.

The epidermis is the outermost layer of the skin, composed mainly of stratified squamous epithelium. It forms a protective barrier that prevents water loss and inhibits the entry of microorganisms. The epidermis contains no blood vessels, and its cells are nourished by diffusion from the underlying dermis. The bottom-most layer of the epidermis, called the stratum basale, is responsible for generating new skin cells that eventually move up to replace dead cells on the surface. This process of cell turnover takes about 28 days in adults.

The most superficial part of the epidermis consists of dead cells called squames, which are constantly shed and replaced. The exact rate at which this happens varies depending on location; for example, it's faster on the palms and soles than elsewhere. Melanocytes, the pigment-producing cells, are also located in the epidermis, specifically within the stratum basale layer.

In summary, the epidermis is a vital part of our integumentary system, providing not only physical protection but also playing a crucial role in immunity and sensory perception through touch receptors called Pacinian corpuscles.

Sweat glands are specialized tubular structures in the skin that produce and secrete sweat, also known as perspiration. They are part of the body's thermoregulatory system, helping to maintain optimal body temperature by releasing water and heat through evaporation. There are two main types of sweat glands: eccrine and apocrine.

1. Eccrine sweat glands: These are distributed throughout the body, with a higher concentration on areas like the palms, soles, and forehead. They are responsible for producing a watery, odorless sweat that primarily helps to cool down the body through evaporation.

2. Apocrine sweat glands: These are mainly found in the axillary (armpit) region and around the anogenital area. They become active during puberty and produce a thick, milky fluid that does not have a strong odor on its own but can mix with bacteria on the skin's surface, leading to body odor.

Sweat glands are controlled by the autonomic nervous system, meaning they function involuntarily in response to various stimuli such as emotions, physical activity, or changes in environmental temperature.

Ichthyosis is a group of skin disorders that are characterized by dry, thickened, scaly skin. The name "ichthyosis" comes from the Greek word "ichthys," which means fish, as the skin can have a fish-like scale appearance. These conditions can be inherited or acquired and vary in severity.

The medical definition of ichthyosis is a heterogeneous group of genetic keratinization disorders that result in dry, thickened, and scaly skin. The condition may affect any part of the body, but it most commonly appears on the extremities, scalp, and trunk. Ichthyosis can also have associated symptoms such as redness, itching, and blistering.

The severity of ichthyosis can range from mild to severe, and some forms of the condition may be life-threatening in infancy. The exact symptoms and their severity depend on the specific type of ichthyosis a person has. Treatment for ichthyosis typically involves moisturizing the skin, avoiding irritants, and using medications to help control scaling and inflammation.

A hair follicle is a part of the human skin from which hair grows. It is a complex organ that consists of several layers, including an outer root sheath, inner root sheath, and matrix. The hair follicle is located in the dermis, the second layer of the skin, and is surrounded by sebaceous glands and erector pili muscles.

The hair growth cycle includes three phases: anagen (growth phase), catagen (transitional phase), and telogen (resting phase). During the anagen phase, cells in the matrix divide rapidly to produce new hair fibers that grow out of the follicle. The hair fiber is made up of a protein called keratin, which also makes up the outer layers of the skin and nails.

Hair follicles are important for various biological functions, including thermoregulation, sensory perception, and social communication. They also play a role in wound healing and can serve as a source of stem cells that can differentiate into other cell types.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Salivary cystatins are a group of proteins that belong to the cystatin superfamily and are found in saliva. They function as inhibitors of cysteine proteases, which are enzymes that break down other proteins. Specifically, salivary cystatins help regulate the activity of these proteases in the oral cavity and protect the soft tissues of the mouth from degradation. There are several types of salivary cystatins, including cystatin A, B, C, D, SN, S, SA, and SB, each with different properties and functions. Some salivary cystatins have been studied for their potential role in oral health and disease, such as caries prevention and protection against oral cancer.

Transglutaminases are a family of enzymes that catalyze the post-translational modification of proteins by forming isopeptide bonds between the carboxamide group of peptide-bound glutamine residues and the ε-amino group of lysine residues. This process is known as transamidation or cross-linking. Transglutaminases play important roles in various biological processes, including cell signaling, differentiation, apoptosis, and tissue repair. There are several types of transglutaminases, such as tissue transglutaminase (TG2), factor XIII, and blood coagulation factor XIIIA. Abnormal activity or expression of these enzymes has been implicated in various diseases, such as celiac disease, neurodegenerative disorders, and cancer.

"Skin physiological phenomena" is not a standard medical term with a specific definition. However, I can provide some information about the general concepts that might be encompassed by this term.

Physiological phenomena refer to the functions and processes that occur in living organisms. When it comes to the skin, there are many different physiological phenomena that take place, including:

1. Barrier function: The skin acts as a barrier to protect the body from external elements such as bacteria, viruses, chemicals, and UV radiation.
2. Temperature regulation: The skin helps regulate body temperature through sweat production and blood flow.
3. Sensation: The skin contains nerve endings that allow us to feel touch, pressure, pain, and temperature.
4. Vitamin D synthesis: The skin can produce vitamin D when exposed to sunlight.
5. Moisture regulation: The skin helps maintain the body's moisture balance by producing sweat and preventing water loss.
6. Immunological function: The skin plays a role in the immune system by providing a physical barrier and containing immune cells that help fight off infections.
7. Excretion: The skin eliminates waste products through sweat.
8. Wound healing: The skin has the ability to repair itself after injury, through a complex process involving inflammation, tissue regeneration, and remodeling.

Therefore, "skin physiological phenomena" could refer to any or all of these functions and processes that take place in the skin.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Kininogens are a group of proteins found in the blood plasma that play a crucial role in the inflammatory response and blood coagulation. They are precursors to bradykinin, a potent vasodilator and inflammatory mediator. There are two types of kininogens: high molecular weight kininogen (HMWK) and low molecular weight kininogen (LMWK). HMWK is involved in the intrinsic pathway of blood coagulation, while LMWK is responsible for the release of bradykinin. Both kininogens are important targets in the regulation of inflammation and hemostasis.

The Amyloid Beta-Protein Precursor (AβPP) is a type of transmembrane protein that is widely expressed in various tissues and organs, including the brain. It plays a crucial role in normal physiological processes, such as neuronal development, synaptic plasticity, and repair.

AβPP undergoes proteolytic processing by enzymes called secretases, resulting in the production of several protein fragments, including the amyloid-beta (Aβ) peptide. Aβ is a small peptide that can aggregate and form insoluble fibrils, which are the main component of amyloid plaques found in the brains of patients with Alzheimer's disease (AD).

The accumulation of Aβ plaques is believed to contribute to the neurodegeneration and cognitive decline observed in AD. Therefore, AβPP and its proteolytic processing have been the focus of extensive research aimed at understanding the pathogenesis of AD and developing potential therapies.

Cathepsin B is a lysosomal cysteine protease that plays a role in various physiological processes, including intracellular protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor (procathepsin B) and activated upon cleavage of the propeptide by other proteases or autocatalytically. Cathepsin B has a wide range of substrates, including collagen, elastin, and various intracellular proteins. Its dysregulation has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Alzheimer's disease is a progressive disorder that causes brain cells to waste away (degenerate) and die. It's the most common cause of dementia — a continuous decline in thinking, behavioral and social skills that disrupts a person's ability to function independently.

The early signs of the disease include forgetting recent events or conversations. As the disease progresses, a person with Alzheimer's disease will develop severe memory impairment and lose the ability to carry out everyday tasks.

Currently, there's no cure for Alzheimer's disease. However, treatments can temporarily slow the worsening of dementia symptoms and improve quality of life.

Transgenic mice are genetically modified rodents that have incorporated foreign DNA (exogenous DNA) into their own genome. This is typically done through the use of recombinant DNA technology, where a specific gene or genetic sequence of interest is isolated and then introduced into the mouse embryo. The resulting transgenic mice can then express the protein encoded by the foreign gene, allowing researchers to study its function in a living organism.

The process of creating transgenic mice usually involves microinjecting the exogenous DNA into the pronucleus of a fertilized egg, which is then implanted into a surrogate mother. The offspring that result from this procedure are screened for the presence of the foreign DNA, and those that carry the desired genetic modification are used to establish a transgenic mouse line.

Transgenic mice have been widely used in biomedical research to model human diseases, study gene function, and test new therapies. They provide a valuable tool for understanding complex biological processes and developing new treatments for a variety of medical conditions.

... cystatin C, a marker of kidney function), CST4, CST5, CST6, CST7, CST8, CST9, CST11, CSTA (cystatin A), CSTB (cystatin B)[ ... Chicken cystatin quickly passed the membrane of MCF-10A neo T cells and inhibited cathepsin B when it was acylated with fatty ... Cystatin: a protein that flips out! Interesting PDB structure article at PDBe Lee C, Bongcam-Rudloff E, Sollner C, Jahnen- ... These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and ...
Cystatin-B is a protein that in humans is encoded by the CSTB gene. The cystatin superfamily encompasses proteins that contain ... "Entrez Gene: CSTB cystatin B (stefin B)". Pavlova, Alona; Björk Ingemar (Sep 2003). "Grafting of features of cystatins C or B ... Pol, E; Björk I (Sep 2001). "Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the ... 1997). "Unstable insertion in the 5' flanking region of the cystatin B gene is the most common mutation in progressive ...
Cystatin-A is a protein that in humans is encoded by the CSTA gene. The cystatin superfamily encompasses proteins that contain ... 1995). "Solution structure of a human cystatin A variant, cystatin A2-98 M65L, by NMR spectroscopy. A possible role of the ... Estrada, S; Nycander M; Hill N J; Craven C J; Waltho J P; Björk I (May 1998). "The role of Gly-4 of human cystatin A (stefin A ... "Entrez Gene: CSTA cystatin A (stefin A)". Pavlova, Alona; Björk Ingemar (Sep 2003). "Grafting of features of cystatins C or B ...
... levels have been reported to be higher in subjects with Alzheimer's disease. The role of cystatin C in multiple ... The cystatin locus on the short arm of chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. The ... Cystatin C is a non-glycosylated, basic protein (isoelectric point at pH 9.3). The crystal structure of cystatin C is ... The role of cystatin C to monitor GFR during pregnancy remains controversial. Like creatinine, the elimination of cystatin C ...
... (HCCAA) is a rare, fatal amyloid disease in young people in Iceland caused by a ... Mutations in the cystatin 3 gene are responsible for the Icelandic type of hereditary cerebral amyloid angiopathy, a condition ... Levy, E; Jaskolski, M; Grubb, A (January 2006). "The role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology ... A, Palsdottir; Ao, Snorradottir; L, Thorsteinsson (January 2006). "Hereditary cystatin C amyloid angiopathy: genetic, clinical ...
Cystatin A Schultz, JE; Matin, A (March 5, 1991). "Molecular and functional characterization of a carbon starvation gene of ...
Cystatin C - Cystatin C is produced in kidney cells and is used as a biomarker. The level of cystatin C is used to determine ... Therefore, a high amount of cystatin C in the blood is a determinant of kidney injury. EGF - lower levels of EGF mRNA and ... "Cystatin C". National Kidney Foundation. 2015-12-24. Retrieved 2020-12-07. Shiva, Niharika; Sharma, Nisha; Kulkarni, Yogesh A ... Kidney ischemia can be diagnosed by checking the levels of several biomarkers such as clusterin and cystatin C. While the ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-F is a protein that in humans is encoded by the CST7 gene. The cystatin superfamily encompasses proteins that contain ... The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ... Ni J, Fernandez MA, Danielsson L, Chillakuru RA, Zhang J, Grubb A, Su J, Gentz R, Abrahamson M (Oct 1998). "Cystatin F is a ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-like 1 is a protein that in humans is encoded by the CSTL1 gene. The cystatin superfamily encompasses proteins that ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located at ... The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ...
... s are members of a family of proteins that evolved from the protein cystatin by gene duplication and exchange of gene ... Fetuins thus belong to the cystatin superfamily of proteins. Fetuin relatives within this superfamily are the histidine-rich ...
They have used cystatin C for estimation of GFR in the clinical routine since 1994. Grubb and coworkers have developed cystatin ... Northern blot studies showed that cystatin C was produced by all nucleated human cells. The biological function of cystatin C ... cystatin C, 13,343Da) than of smaller ones (e.g. creatinine, 113Da) and identified by a greater reduction of the cystatin C- ... IFCC Working Group on Standardisation of Cystatin C (WG-SCC) (2010). "First certified reference material for cystatin C in ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-M is a protein that in humans is encoded by the CST6 gene. The cystatin superfamily encompasses proteins that contain ... 2006). "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the ... The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, ...
2008). "Cystatin C-cathepsin B axis regulates amyloid beta levels and associated neuronal deficits in an animal model of ... Their study indicated complex roles of cystatin C (CysC); CysC inhibits CatB degradation of Aβ peptides, but CysC itself ...
The results show that cystatin B has a polymeric structure, and that the mutated form of cystatin B, which is present in ... Current research links cystatin B to production of inhibitory neurons known as GABAergic neurons. It has shown that a lack of ... Cystatin B and its EPM1 mutants are polymeric and aggregate prone in vivo. Biochimica et Biophysica Acta 1783: 312-22 Ferlazzo ... It is caused due to a mutation in the cystatin B gene (CSTB). The disease is named after Heinrich Unverricht, who first ...
Cystatin C is freely filtered at the glomerulus. After filtration, Cystatin C is reabsorbed and catabolized by the tubular ... Cystatin C levels are therefore measured not in the urine, but in the bloodstream. Equations have been developed linking ... One of these is cystatin C, a ubiquitous protein secreted by most cells in the body (it is an inhibitor of cysteine protease).[ ... The most accurate is (sex, age and race) adjusted cystatin C, followed by (sex, age and race) adjusted creatinine and then ...
"Functional characterization of a cystatin from the tick Rhipicephalus haemaphysaloides". Parasites & Vectors. 8: 140. doi: ...
... cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of ... 1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-S is a protein that in humans is encoded by the CST4 gene. The cystatin superfamily encompasses proteins that contain ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-D is a protein that in humans is encoded by the CST5 gene. The cystatin superfamily encompasses proteins that contain ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ... The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. ...
The fourth group are cystatin proteins, which will inhibit cysteine proteases. These will inhibit the breakdown of the proteins ...
... cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of ... 1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-SN is a protein that in humans is encoded by the CST1 gene. The cystatin superfamily encompasses proteins that contain ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-8 is a protein that in humans is encoded by the CST8 gene. The cystatin superfamily encompasses proteins that contain ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ... "Entrez Gene: CST8 cystatin 8 (cystatin-related epididymal specific)". The MEROPS online database for peptidases and their ...
... cystatin SN, cystatin SA, cystatin S, and two phosphorylated forms of cystatin S) in human whole saliva and determination of ... 1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-SA is a protein that in humans is encoded by the CST2 gene. The cystatin superfamily encompasses proteins that contain ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... Cystatin-9-like is a protein that in humans is encoded by the CST9L gene. The cystatin superfamily encompasses proteins that ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ... "Entrez Gene: CST9L cystatin 9-like (mouse)". Brown WM, Dziegielewska KM (1997). "Friends and relations of the cystatin ...
1989). "Cystatin superfamily. Evidence that family II cystatin genes are evolutionarily related to family III cystatin genes". ... The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in ... Cystatin-11 is a protein that in humans is encoded by the CST11 gene. The cystatin superfamily encompasses proteins that ... 2002). "Cystatin 11: a new member of the cystatin type 2 family". Endocrinology. 143 (7): 2787-96. doi:10.1210/endo.143.7.8925 ...
Staphopain A is inhibited by phosphorylated cystatin α and α2-macroglobulin. Staphopain A can cleave and lower the activity α1- ... Inhibition of staphopain A by phosphorylated cystatin α did prevent colony formation in skin tissue, but the effect could also ... "Inhibition of cysteine protease and growth of Staphylococcus aureus V8 and poliovirus by phosphorylated cystatin alpha ... properties of peptidyl derivatives and cyclopeptides structurally based upon the inhibitory centre of human cystatin C. ...
Juliana F. Roos; Jenny Doust; Susan E. Tett; Carl M.J. Kirkpatrick (2007). "Diagnostic accuracy of cystatin C compared to serum ... serum cystatin C or equations?". Clinical Biochemistry. 40 (3-4): 153-161. doi:10.1016/j.clinbiochem.2006.10.014. PMID 17234172 ...
Inker, Lesley (2021). "New Creatinine- and Cystatin C-Based Equations to Estimate GFR without Race". New England Journal of ... Inker, Lesley (2012). "Estimating Glomerular Filtration Rate from Serum Creatinine and Cystatin C". New England Journal of ... cystatin C, and panels of metabolites and low molecular weight proteins. The 2009 creatinine equation with race and the 2021 ...
Finney H, Newman DJ, Price CP (January 2000). "Adult reference ranges for serum cystatin C, creatinine and predicted creatinine ...
Estrada, S; Nycander M; Hill N J; Craven C J; Waltho J P; Björk I (May 1998). "The role of Gly-4 of human cystatin A (stefin A ... 1998). "The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and ... CTSL1 has been shown to interact with Cystatin A. Cathepsin L has been reported in many organisms including fish, birds, ... Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, ...
In addition to a mutation in a stop codon, a splice site mutation on the 3' strand was found in a gene coding for cystatin B in ... This transversion occurs in the region that codes for the cystatin B gene. Individuals suffering from Progressive Myoclonus ... "Mutations in the Gene Encoding Cystatin B in Progressive Myoclonus Epilepsy (EPM1)". Science. 271 (5256): 1731-1734. Bibcode: ...
... cystatin C, a marker of kidney function), CST4, CST5, CST6, CST7, CST8, CST9, CST11, CSTA (cystatin A), CSTB (cystatin B)[ ... Chicken cystatin quickly passed the membrane of MCF-10A neo T cells and inhibited cathepsin B when it was acylated with fatty ... Cystatin: a protein that flips out! Interesting PDB structure article at PDBe Lee C, Bongcam-Rudloff E, Sollner C, Jahnen- ... These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and ...
Data from the Beaver Dam Eye Study show a relationship between the level of serum cystatin C and chronic kidney disease with ... "Serum cystatin C has been used to estimate glomerular filtration rate to define the presence of CKD," write Ronald Klein, MD, ... The goal of this study was to examine the associations of the serum cystatin C level and chronic kidney disease with the ... After controlling for age and other risk factors, the level of serum cystatin C at baseline was associated with the incidence ...
myADLM.org // ... // Clinical Chemistry Journal // Clinical Case Studies // Cystatin C for Therapeutic Drug Monitoring ... the measurement of serum cystatin C (CysC) was recommended to detect a possibly impaired renal function. Pending this ...
Cystatin Cs Naughty Side-Slowing Aβ Degradation by Cathepsin B. Quick Links. *Article ... At first glance, this trend would seem to back recent work indicating a seemingly beneficial role for cystatin C in AD mice-as ... As suggested by several studies (Benussi et al., 2003; Paraoan et al., 2004), a cystatin C variant (A25T) that is associated ... "In humans, the evidence is that reducing cystatin C levels puts you at risk for AD," said Paul Mathews of the Nathan Kline ...
blood cystatin level + The amount of any cystatin (that is, of any member of the cystatin superfamily of proteins, many of ... blood cystatin level (CMO:0002776). Annotations: Rat: (0) Mouse: (0) Human: (0) Chinchilla: (0) Bonobo: (0) Dog: (0) Squirrel ...
... ... Equations that include cystatin C predict GFR more accurately than serum creatinine in children, adults, and older adults with ... Furthermore, cystatin C offers the opportunity to avoid the race coefficient that is required for any current creatinine-based ... The goal of this update is to raise awareness of clinical scenarios where cystatin C has clear and immediate benefits as an ...
SSCYSCR - Cystatin C (mg/L) - REPEAT. Variable Name: SSCYSCR. SAS Label: Cystatin C (mg/L) - REPEAT. English Text: Cystatin C ( ... Cystatin C, BTP and B2M were measured in 2009 at the University of Minnesota (1, 2). Cystatin C measurements were conducted ... Cystatin C, ß-trace Protein & ß2 Microglobulin - Serum (NHANES III Surplus), Second Exam (SSNH3CYS) Data File: SSNH3CYS.xpt ... Cystatin C, β-trace protein (BTP) and β2 microglobulin (B2M) assayed from stored surplus serum samples from the NHANES III ...
Mark Cystatin C-Based Equation to Estimate GFR without the Inclusion of Race and Sex Pottel, Hans ; Björk, Jonas LU ; Rule, ... Remove department: Cystatin C, renal disease, amyloidosis and antibiotics Built with LibreCat User guide , About accessibility ... Mark Muscle mass, creatinine, cystatin C, and selective glomerular hypofiltration syndromes Malmgren, Linnea LU and Grubb, ... Mark Cystatin C-based equations for estimating glomerular filtration rate do not require race or sex coefficients. Ottosson ...
Cystatin 6 (CST6) ELISA Kit DIY Materials. Cat# MBS2089402. Supplier: MyBiosource. Available at Gentaur Genprice in 5 to 7 ... Product Name Synonyme: [Cystatin E/M]. Other Names: [cystatin-M; Cystatin-M; cystatin-M; cystatin E/M; Cystatin-6; Cystatin-E] ... MBS2089402 , Cystatin 6 (CST6) ELISA Kit DIY Materials MyBiosource Elisa Kits MBS2089402 , Cystatin 6 (CST6) ELISA Kit DIY ... MBS2089402 , Cystatin 6 (CST6) ELISA Kit DIY Materials. Rating Required Select Rating. 1 star (worst). 2 stars. 3 stars ( ...
A cystatin C (cys)-based European Kidney Function Consortium (EKFC) equation has similar accuracy to the creatinine (cr)-based ... Use of cystatin C for precise assessment of kidney function and cardiovascular risk. Jun 9, 2020 ... A cystatin C (cys)-based European Kidney Function Consortium (EKFC) equation has similar accuracy to the creatinine (cr)-based ... More information: Hans Pottel et al, Cystatin C-Based Equation to Estimate GFR without the Inclusion of Race and Sex, New ...
Zurdel et al chose as a potential candidate the cystatin C gene-CST3-coding for a protease inhibitor common in tissues and body ... CST3 B/B carries increased risk of exudative ARMD, conclude Zudel et al; cystatin C is therefore implicated in the disease ...
The serum level of cystatin C is stable and it can reflect renal function sensitively. The study aimed to assess the usefulness ... of cystatin C for early diagnosis of contrast-induced nephropathy in patients undergoing coronary angiography. MATERIAL AND ... Significance of Cystatin C for Early Diagnosis of Contrast-Induced Nephropathy in Patients Undergoing Coronary Angiography DOI ...
The range of serum cystatin C values was 1,2±0,42 mg/L in control dogs, 2,96±1,09 mg/L in dogs with azotaemic renal disease (p, ... Various studies have reported about cystatin C as an easy and rapid assessable marker that can be used for accurate information ... Evaluation of Glomerular Filtration Rate in Dogs with Renal Disease Using Serum Cystatin C ... of 30 dogs of different breeds with a broad range of bodyweight were evaluated by using serum cystatin C to determine its ...
Examining the utility of cystatin C as a confirmatory test of chronic kidney disease across the age range in middle-aged and ... Examining the utility of cystatin C as a confirmatory test of chronic kidney disease across the age range in middle-aged and ...
Cystatin A, also known as Stefin A, Cystatin AS or Keratolinin, is a member of family 1 of the cystatin superfamily. It is a 98 ...
... based on cystatin-based CKD compared to participants without CKD. In general, the HRs were higher for cystatin C-based CKD ... Especially in low-risk settings, the use of cystatin C-based CKD may result in more accurate risk estimates and have better ... Routinely, creatinine has been used as the main marker of renal function, but recently, cystatin C emerged as a more promising ... The overall prevalence of CKD stage 3-5 by creatinine- and cystatin C-based eGFR, respectively, was 3.3% and 7.4% in the ...
Serum cystatin C concentrations (sCysC) might be less influenced by changes in body muscle mass and so better indicate the ... Serum cystatin C concentrations (sCysC) might be less influenced by changes in body muscle mass and so better indicate the ... Serum Cystatin C Concentrations in Cats with Hyperthyroidism and Chronic Kidney Disease. ...
Muscle mass, creatinine, cystatin C, and selective glomerular hypofiltration syndromes. / Malmgren, Linnea; Grubb, Anders. ... Muscle mass, creatinine, cystatin C, and selective glomerular hypofiltration syndromes. Clinical Kidney Journal. 2023 apr. doi ... Muscle mass, creatinine, cystatin C, and selective glomerular hypofiltration syndromes. I: Clinical Kidney Journal. 2023. ... Malmgren, L., & Grubb, A. (2023). Muscle mass, creatinine, cystatin C, and selective glomerular hypofiltration syndromes. ...
... dc.contributor.author. van der Laan, SW. en_US. ... van der Laan Cystatin C and .... Size:. 963.4Kb. Format:. application/. Description:. Accepted version. ...
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Cystatin - C. July 25, 2023. Immunoassay Test Name:. Cystatin - C. Description:. Test: Cystatin - C. MRP: 2300. Parameters: ...
Cystatin C. Cystatin C is a small non-glycosylated protein produced by all human nucleated cells, filtered freely at the ... Cystatin C. Cystatin C is a 13-kD cysteine protease inhibitor that has gained popularity for measuring kidney function and ... Cystatin C has a superior correlation with GFR compared with serum creatinine as measured by iohexol clearance. [77] Given that ... Cystatin C and the risk of death and cardiovascular events among elderly persons. N Engl J Med. 2005 May 19. 352 (20):2049-60. ...
... cystatin 3; cystatin C (amyloid angiopathy and cerebral hemorrhage); Cystatin C; cystatin-3; cystatin-C; Gamma-trace; MGC117328 ... cystatin 3; cystatin C (amyloid angiopathy and cerebral hemorrhage); Cystatin C; cystatin-3; cystatin-C; Gamma-trace; MGC117328 ... Target Cystatin C * Specificity This human Cystatin C ELISA assay is reactive to cystatin C in human samples. There is no ... HEL-S-2 cystatin C cystatin-C,bA218C14.4 (cystatin C),cystatin 3,epididymis secretory protein Li 2,gamma-trace,neuroendocrine ...
Cystatin C is freely filtered in the renal glomeruli and is normally re-absorbed in the proximal tubules where it is nearly ... Cystatin C is used as a measure of glomerular filtration rate (GFR) in patients where creatinine results may be misleading, ... The proportion of cystatin C found in the serum is inversely proportional to the glomerular filtration rate and is uanaffected ... Cystatin C is useful for assessing renal function in patients suspected of having kidney disease, and monitoring treatment ...
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The Cystatin C Human ELISA kit is designed to quantitatively measure human Cystatin C present in biological samples and tissue ... Cystatin C Human ELISA Kit The DetectX Cystatin C Immunoassay Kit is designed to measure Human Cystatin C levels in a variety ... Cystatin C Human ELISA Kit. The DetectX Cystatin C Immunoassay Kit is designed to measure Human Cystatin C levels in a variety ... Cystatin C is a low molecular weight non-glycosylated protein (13 kDa) in the cystatin superfamily. Cystatin C belongs to the ...
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mouse Cystatin B CSTB antibody validated for ELISA,Western Blot ...
  • Serum cystatin C has been used to estimate glomerular filtration rate to define the presence of CKD," write Ronald Klein, MD, MPH, from the University of Wisconsin School of Medicine and Public Health, Madison, and colleagues. (medscape.com)
  • Casual blood specimens were obtained at each examination to determine white blood cell count, serum blood urea nitrogen, glomerular filtration rate, and cystatin C. The glomerular filtration rate from serum creatinine was estimated using the Modification of Diet in Renal Disease (Study) prediction equation. (medscape.com)
  • The goal of this update is to raise awareness of clinical scenarios where cystatin C has clear and immediate benefits as an alternative glomerular filtration rate (GFR) biomarker to supplement creatinine. (lww.com)
  • A cystatin C (cys)-based European Kidney Function Consortium (EKFC) equation has similar accuracy to the creatinine (cr)-based equation for estimating glomerular filtration rate (GFR), according to a study published in the Jan. 26 issue of the New England Journal of Medicine . (medicalxpress.com)
  • For this reason in this study, the glomerular filtration rate (GFR) of 30 dogs of different breeds with a broad range of bodyweight were evaluated by using serum cystatin C to determine its usefulness as a marker. (vin.com)
  • In this editorial, the simultaneous use of creatinine and cystatin C to estimate GFR, muscle mass and selective glomerular hypofiltration syndromes is described. (lu.se)
  • Glomerular filtration in the kidneys removes Cystatin C from the blood plasma. (arborassays.com)
  • A linear relationship exists between the reciprocal Cystatin C concentration in plasma and the glomerular filtration rate (GFR). (arborassays.com)
  • The cystatin-c test analyses the working of the kidney by measuring the glomerular filtration rate. (redcliffelabs.com)
  • Cystatin C, also known as Cystatin-3 (CST3) is a secreted type 2 cysteine protease inhibitor synthesized in all nucleated cells, has been proposed as a replacement for serum creatinine for the assessment of renal function, particularly to detect small reductions in glomerular filtration rate. (betalifesci.com)
  • Indeed, the concentration of Cystatin C is mainly determined by glomerular filtration and is particularly of interest in clinical settings where the relationship between creatinine production and muscle mass impairs the clinical performance of creatinine. (betalifesci.com)
  • Inker et al reported equations for estimating glomerular filtration rate (eGFR) based on serum cystatin C concentrations, age and gender. (medicalalgorithms.com)
  • Comparison of Cystatin C and Creatinine-Based Equations with Measured Glomerular Filtration Rate in a Diverse Pediatric Population. (bvsalud.org)
  • While measured glomerular filtration rate (mGFR) is occasionally used as a reference, estimated GFR (eGFR) from serum creatinine - and cystatin C (CysC)-based equations are routinely used in clinical practice as a reliable and less invasive approach. (bvsalud.org)
  • Furthermore, cystatin C offers the opportunity to avoid the race coefficient that is required for any current creatinine-based eGFR equation, which has been appropriately criticized for introducing unnecessary imprecision, assumptions and values on GFR estimation. (lww.com)
  • Mean (standard deviation) molybdenum-corrected urine cadmium , Modification of Diet in Renal Disease (MDRD) eGFR and multi-variable cystatin C eGFR were 1.02 (0.65) ug/g creatinine, and 97.4 (19.2) and 112.0 (17.7) mL/min/1.73 m2, respectively. (cdc.gov)
  • Because it has been proven that in advanced liver diseases or liver cirrhosis an overestimation of the GFR occurs when sCr is used, the measurement of serum cystatin C (CysC) was recommended to detect a possibly impaired renal function. (aacc.org)
  • In the October 23 Neuron, Gan and colleagues now report that APP mice lacking cystatin C (CysC)-an inhibitor of cysteine proteases including CatB-have lower soluble Aβ levels and reduced Aβ-associated deficits in cognition, behavior, and synaptic plasticity compared to APP/CysC+/+ mice. (alzforum.org)
  • The amount of any cystatin (that is, of any member of the cystatin superfamily of proteins, many of which act as cysteine protease inhibitors) found in a specified sample of blood, the fluid that circulates through the heart, arteries, capillaries and veins carrying nutrients and oxygen to the body tissues and metabolites away from them. (mcw.edu)
  • Cystatin A, also known as Stefin A, Cystatin AS or Keratolinin, is a member of family 1 of the cystatin superfamily. (reliatech.de)
  • Cystatin C is a low molecular weight non-glycosylated protein (13 kDa) in the cystatin superfamily. (arborassays.com)
  • We compared associations of urine cadmium with kidney function measures based on serum cystatin C to those with serum creatinine in 712 lead workers. (cdc.gov)
  • Zurdel et al chose as a potential candidate the cystatin C gene- CST3 -coding for a protease inhibitor common in tissues and body fluids which strongly inhibits cathepsins, including cathepsin S, and results in debris accumulating around retinal pigment epithelial cells. (bmj.com)
  • Cystatin C belongs to the cysteine proteinase inhibitor group. (arborassays.com)
  • To analyze the contribution of cysteine proteases to metastasis we have over-expressed in B16 melanoma cells the natural cysteine protease inhibitor, cystatin C. We measured in vitro invasion of cystatin over-expression clones with Boyden chamber type assays. (biomedcentral.com)
  • Cystatin C is a type II cysteine protease inhibitor that is normally secreted from cells [ 10 ]. (biomedcentral.com)
  • Cystatin C is an inhibitor of cathepsins. (eucys2017.eu)
  • Cystatin C, a cysteine protease inhibitor, was subject to hydrolysis at two sites when complexed with papain and in the presence of excess papain. (mcmaster.ca)
  • A pH-dependent conformational variability in this region of the inhibitor could explain the differences in the X-ray crystallographic and n.m.r. structures of the homologous chicken cystatin. (mcmaster.ca)
  • Cystatin A (Cys A), a cysteine protease inhibitor, is a precursor of proteins involves in keratinocyte keratinization, and is expressed during the late phase of differentiation of these cells. (bvsalud.org)
  • We used the common variant rs911119 in CST3 as an instrumental variable to investigate the causal role of cystatin C in CVD, including coronary heart disease, ischemic stroke, and heart failure. (scilifelab.se)
  • Mendelian randomization analyses did not support a causal role of cystatin C in the etiology of CVD. (scilifelab.se)
  • In this study we show over-expression of cystatin C in melanoma cells is associated with reduced metastasis and increased apoptosis in lung tissues. (biomedcentral.com)
  • The expression of cystatin C-GFP fusion was observed in B16F10 melanoma cells following transient transfection of plasmid construct DNA. (biomedcentral.com)
  • Studies suggest that expression of cystatin A is inversely associated with malignant progression of cancer 9 . (bvsalud.org)
  • This indicates that at physiological ionic strength of 0.15 M, a significant proportion of cystatin C complexed with protease would be in a proteolytically labile conformation over the pH range 4.5 to 5, which is encountered in lysosomes. (mcmaster.ca)
  • In light of prior human polymorphism data and recent mouse data highlighting cystatin C's ability to interfere with amyloid aggregation, the new findings suggest a more complex character for cystatin C and make it challenging to say whether it plays a "good" or "bad" role in AD pathogenesis. (alzforum.org)
  • At first glance, this trend would seem to back recent work indicating a seemingly beneficial role for cystatin C in AD mice-as an agent that interferes with amyloid aggregation (see ARF related news story ). (alzforum.org)
  • The imbalance between Cystatin C and cysteine proteinases is associated with conditions such as cancer, Alzheimer's disease, multiple sclerosis, and hereditary Cystatin C amyloid angiopathy. (arborassays.com)
  • Scholars@Duke publication: Cystatin C mutation in an elderly man with sporadic amyloid angiopathy and intracerebral hemorrhage. (duke.edu)
  • BACKGROUND: Cerebral amyloid angiopathy (CAA) with intracerebral hemorrhage (ICH) occurs both sporadically and as a result of mutations in either cystatin C or the amyloid precursor protein. (duke.edu)
  • citation needed] The cystatin family includes: The Type 1 cystatins, which are intracellular and are present in the cytosol of many cell types, but can also appear in body fluids at significant concentrations. (wikipedia.org)
  • vancomycin was the most frequently studied drug and its target level and elimination were better predicted by cystatin C. Overall, approaches to medication dosing and monitoring that include cystatin C concentrations have been shown to result in a better achievement of drug trough levels. (lww.com)
  • Serum cystatin C concentrations (sCysC) might be less influenced by changes in body muscle mass and so better indicate the presence of concurrent chronic kidney disease (CKD) in hyperthyroidism. (avmi.net)
  • ELISA) was used to determine the concentrations of serum pentraxin-3 and cystatin C. Utilizing SPSS version 22, statistical analysis was conducted. (pafmj.org)
  • The CST3 BB genotype and low cystatin C cerebrospinal fluid levels are associated with dementia in Lewy body disease. (nih.gov)
  • Product Description google Human Cystatin C ELISA Kit (DIY Antibody Pairs) (antibody pairs and standards for assay development). (biosensis.com)
  • Specificity This human Cystatin C ELISA assay is reactive to cystatin C in human samples. (biosensis.com)
  • The Cystatin C Human ELISA Kit quantitatively measures Human Cystatin C levels in serum, plasma (EDTA and Heparin), urine, and tissue culture media. (arborassays.com)
  • Use our provided human Cystatin C standard to generate a standard curve for the assay. (arborassays.com)
  • Pipette the standards or diluted samples into a transparent microtiter plate coated with our mouse anti-human Cystatin C antibody and incubate at room temperature for 1 hour. (arborassays.com)
  • Add the peroxidase-conjugated human Cystatin C monoclonal antibody. (arborassays.com)
  • The mature, active form of human cystatin C is a single non-glycosylated polypeptide chain consisting of 12 amino acid residues, with a molecular mass of 13,343-13,359 Da, and containing four characteristic disulfide-paired cysteine residues. (betalifesci.com)
  • A DNA sequence encoding the human Cystatin-C (NP_000090.1) (Ser 27-Ala 146) was expressed with a C-terminal His tag. (betalifesci.com)
  • The mature recombinant human Cystatin-C consists of 131 a.a. and predicts a molecular mass of 14.8 kDa. (betalifesci.com)
  • Description: A competitive ELISA for quantitative measurement of Human Cystatin SN(CST1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (cromauv.org)
  • Evaluate the levels of serum pentraxin-3 and human cystatin C in migraine patients and the relationship between various parameters in migraine patients to healthy controls. (pafmj.org)
  • CASE DESCRIPTION: We report a case of sporadic CAA with ICH in an elderly Croatian man with a mutation in cystatin C identical to that found in Icelandic hereditary cerebral hemorrhage with amyloidosis. (duke.edu)
  • Cystatin: a protein that flips out! (wikipedia.org)
  • Cystatin C, β-trace protein (BTP) and β2 microglobulin (B2M) assayed from stored surplus serum samples from the NHANES III Second Examination (1988-1994). (cdc.gov)
  • To help establish mechanism of cystatin C action in metastasis we have fused cystatin C to the N-terminus of green fluorescent protein. (biomedcentral.com)
  • Confocal microscopy was used in an attempt to localize cystatin C-GFP protein expression in cells. (biomedcentral.com)
  • This pattern of expression was not anticipated since cystatin C is primarily a secreted protein that should have produced a vesicular localization of fluorescence within the cell. (biomedcentral.com)
  • Figure 2 shows expression of the cystatin C-GFP fusion protein. (biomedcentral.com)
  • Cystatin C is a low-molecular-weight protein which has been proposed as a marker of renal function that could replace creatinine. (betalifesci.com)
  • In almost all the clinical studies, Cystatin C demonstrated a better diagnostic accuracy than serum creatinine in discriminating normal from impaired kidney function, but controversial results have been obtained by comparing this protein with other indices of kidney disease, especially serum creatinine-based equations, such as early atherosclerosis, Alzheimer's dementia, vascular aneurysms, hyperhomocysteinaemia and other neurodegenerative diseases. (betalifesci.com)
  • Cystatin C is a protein that is produced by the cells in your body. (kidney.org)
  • The Cystatin C Human ELISA Kit is a sandwich ELISA with a run time of 2 hours. (arborassays.com)
  • Description: A competitive ELISA for quantitative measurement of Rat Cystatin SN(CST1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (cromauv.org)
  • Equations that include cystatin C predict GFR more accurately than serum creatinine in children, adults, and older adults with larger effects among persons who are acutely ill. (lww.com)
  • Cystatins show similarity to fetuins, kininogens, histidine-rich glycoproteins and cystatin-related proteins. (wikipedia.org)
  • These are cystatin-like proteins found in a range of organisms: plant phytocystatins, fetuin in mammals, insect cystatins, and a puff adder venom cystatin, which inhibits metalloproteases of the MEROPS peptidase family M12 (astacin/adamalysin). (wikipedia.org)
  • Rescaled serum creatinine in the EKFC eGFRcr equation was replaced with rescaled cystatin C, and the resulting EKFC eGFRcys equation was validated in cohorts of White and Black patients in Europe, the United States, and Africa. (medicalxpress.com)
  • Cystatin C serum concentration is not affected by age, gender, or body mass, suggesting it may be a better marker for GFR than serum creatinine. (arborassays.com)
  • Differences in urine cadmium associations with kidney outcomes based on serum creatinine and cystatin C. (cdc.gov)
  • Urine creatinine was associated with serum creatinine-based but not cystatin-C-based eGFRs. (cdc.gov)
  • This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse) immunized with human recombinant Cystatin-A. (reliatech.de)
  • After the 30-minute incubation, wash away the excess peroxidase-conjugated Cystatin C monoclonal antibody and add the TMB substrate. (arborassays.com)
  • The TMB substrate reacts with the bound peroxidase-conjugated Cystatin C monoclonal antibody generating a signal detected by a plate reader at 450nm. (arborassays.com)
  • Clinical utility of serum cystatin C in predicting coronary artery disease in patients without chronic kidney disease. (nih.gov)
  • Cystatin C is freely filtered in the renal glomeruli and is normally re-absorbed in the proximal tubules where it is nearly completely metabolised, leading to insignificant levels in the urine. (chl.co.nz)
  • Hospital laboratories must make cystatin C available for clinical care to improve the safety and efficacy of medications that have narrow therapeutic windows. (lww.com)
  • Cystatin C calibration has varied substantially across laboratories between 2006-when the original NHANES III (First Examination) cystatin C stored surplus sera study was conducted -and 2009-when the present measurements were conducted. (cdc.gov)
  • Users need to consider the shift in laboratories when comparing cystatin C measurements from the Second Examination samples to measurements from the First Examination and other NHANES samples, conducted at different time points. (cdc.gov)
  • Also, a number of the cystatin-like proteins have been shown to be devoid of inhibitory activity. (wikipedia.org)
  • Creatinine-cystatin C ratio and mortality in cancer patients: a retrospective cohort study. (nih.gov)
  • Epidemiological studies show that high circulating cystatin C is associated with risk of cardiovascular disease (CVD), independent of creatinine-based renal function measurements. (scilifelab.se)
  • February 27, 2009 - Serum cystatin C level and chronic kidney disease may have a link to incidence of age-related macular degeneration (AMD) that is independent of smoking and other risk factors, according to a population-based cohort study reported in the February issue of the Archives of Ophthalmology . (medscape.com)
  • The goal of this study was to examine the associations of the serum cystatin C level and chronic kidney disease with the incidence and progression of AMD during 15 years of follow-up in 4926 participants of the Beaver Dam Eye Study. (medscape.com)
  • Use the intensity and the standard curve to calculate the Cystatin C concentration in the samples. (arborassays.com)
  • A decreased concentration of cystatin C in the blood circulation. (nih.gov)
  • The purpose of the present study was to evaluate serum canine Cystatin-C (Cys-C) concentration for the prediction of renal function (RF) in dogs naturally infected with Babesia canis vogeli and Ehrlichia canis. (omu.edu.tr)
  • No significant cross-reactivity or interference between Cystatin 6 (CST6) and analogues was observed. (biocheminfo.org)
  • The Abs in the kit have high sensitivity and excellent specificity for detection of Cystatin 6 (CST6). (biocheminfo.org)
  • Various studies have reported about cystatin C as an easy and rapid assessable marker that can be used for accurate information on renal function impairment in humans lastly, but we have found only one study in dogs. (vin.com)
  • A new marker of GFR, cystatin C, introduced in 1979, has been shown to be virtually uninfluenced by muscle mass. (lu.se)
  • Hans Pottel et al, Cystatin C-Based Equation to Estimate GFR without the Inclusion of Race and Sex, New England Journal of Medicine (2023). (medicalxpress.com)
  • The inter-assay coefficients of variation for the cystatin C, βTP and β2M assays were 4.0% (mean 0.698 mg/L), 5.7% (mean 0.594 mg/L) and 2.7% (mean 1.757 mg/L), respectively. (cdc.gov)
  • Due to differences in laboratory calibration of assays, there are systematic differences in the cystatin C values from the First Examination and those from the Second Examination and other NHANES surveys. (cdc.gov)
  • Hans Pottel, Ph.D., from KU Leuven Campus Kulak Kortrijk in Belgium, and colleagues used data from patients in Sweden to estimate the rescaling factor for cystatin C level in adults. (medicalxpress.com)
  • Cystatin C could be a useful clinical tool to identify HIV-infected persons. (betalifesci.com)
  • Cystatin C measurements were conducted using the Siemens (formerly Dade Behring) N Latex Cystatin C assay, an automated particle-enhanced nepholometric assay (Siemens Diagnostics). (cdc.gov)
  • Chicken cystatin quickly passed the membrane of MCF-10A neo T cells and inhibited cathepsin B when it was acylated with fatty acyl residues of 6-18 carbon atoms. (wikipedia.org)
  • Association of Cystatin C Kidney Function Measures With Long-term Deficit-Accumulation Frailty Trajectories and Physical Function Decline. (nih.gov)
  • It can also be calculated using your cystatin C level. (kidney.org)