Amyloid fibrils are protein polymers comprising identical monomer units (homopolymers). (medscape.com)
Amyloidosis is a clinical disorder caused by extracellular and/or intracellular deposition of insoluble abnormal amyloid fibrils that alter the normal function of tissues. (medscape.com)
[ 5 ] Only 10% of amyloidosis deposits consist of components such as glycosaminoglycans (GAGs), apolipoprotein-E (apoE), and serum amyloid P-component (SAP), while nearly 90% of the deposits consist of amyloid fibrils that are formed by the aggregation of misfolded proteins. (medscape.com)
[ 6 ] In humans, about 23 different unrelated proteins are known to form amyloid fibrils in vivo. (medscape.com)
The modern era of amyloidosis classification began in the late 1960s with the development of methods to solubilize amyloid fibrils. (medscape.com)
Although the accumulation of amyloidogenic proteins in neuroinflammatory conditions is generally considered pathologic, in a murine model of multiple sclerosis, amyloid-forming fibrils, comprised of hexapeptides, are anti-inflammatory. (phoenixpeptide.com)
However, there are number of cases in which the favorable states of proteins are rather unfolded, partially folded (e.g., "molten globular"), or misfolded (e.g., nonspecific aggregates or amyloid fibrils). (tau.ac.il)
The amyloidoses are referred to with a capital A (for amyloid) followed by an abbreviation for the fibril protein. (medscape.com)
Aggregates1
Amyloidosis results from the accumulation of pathogenic amyloids-most of which are aggregates of misfolded proteins-in a variety of tissues. (medscape.com)
Functional3
Functional amyloids play a beneficial role in a variety of physiologic processes (eg, long-term memory formation, gradual release of stored peptide hormones). (medscape.com)
Evaluation of the new F23R variant demonstrated inhibition of β-sheet structure and, therefore, amyloid formation on the native C-terminal, phenomenon that was associated with functional optimization in calcium and cholesterol management coupled with the optimization of insulin secretion by beta cells. (phoenixpeptide.com)
To directly assess the functional effects of these mutations, site-directed mutant receptors were transiently expressed in CHO-K1 cells and cAMP accumulation stimulated by recombinant eelLH (rec-eelLH) was measured by homogeneous time-resolved fluorescence (HTRF) assays. (preprints.org)
Metabolism4
Modulation of Amyloidogenesis Controlled by the C-Terminal Domain of Islet Amyloid Polypeptide Shows New Functions on Hepatocyte Cholesterol Metabolism. (phoenixpeptide.com)
In addition, it was found that C-terminal sequences of IAPP could modulate cholesterol metabolism in hepatocytes through regulation of SREBP-2, apoA-1, ABCA1, and LDLR, mechanism that may represent a new function of IAPP on the metabolism of cholesterol, increasing the LDL endocytosis in hepatocytes. (phoenixpeptide.com)
Our data suggest a new IAPP function associated with rearrangements on metabolism of cholesterol in hepatocytes. (phoenixpeptide.com)
Type1
All types of amyloid consist of one major fibrillar protein that defines the type of amyloid. (medscape.com)
Member1
Luteinizing hormone receptor (LHR) is a member of the seven-transmembrane (TM) receptor family. (preprints.org)
IAPP4
The amyloidogenic region of IAPP is responsible for providing a toxic conformational structure within islets. (phoenixpeptide.com)
In addition, it was found that C-terminal sequences of IAPP could modulate cholesterol metabolism in hepatocytes through regulation of SREBP-2, apoA-1, ABCA1, and LDLR, mechanism that may represent a new function of IAPP on the metabolism of cholesterol, increasing the LDL endocytosis in hepatocytes. (phoenixpeptide.com)
Our data suggest a new IAPP function associated with rearrangements on metabolism of cholesterol in hepatocytes. (phoenixpeptide.com)
Amyloidogenic1
Although the accumulation of amyloidogenic proteins in neuroinflammatory conditions is generally considered pathologic, in a murine model of multiple sclerosis, amyloid-forming fibrils, comprised of hexapeptides, are anti-inflammatory. (phoenixpeptide.com)
Amylin1
Hence, in a murine model of systemic inflammation, pretreatment with amylin hexapeptide reduced mortality, disease severity, and preserved lung barrier function. (phoenixpeptide.com)
Amorphous1
Amorphous eosinophilic interstitial amyloid observed on a renal biopsy. (medscape.com)
Pathogenic2
Amyloidosis results from the accumulation of pathogenic amyloids-most of which are aggregates of misfolded proteins-in a variety of tissues. (medscape.com)
Consistent with the co-localisation of hIAPP and Aβ within the brain, in vitro studies have demonstrated that hIAPP interacts with Aβ, functioning as a seed to promote aggregation, indicating its potential pathogenic role in promoting Aβ cross-seeding and amyloid deposition in AD and T2D 18 . (nature.com)
4] It is also important to understand that the same polypeptide sequence can produce many different patterns of interresidue or intraresidue interactions. (medscape.com)
Evaluation of the new F23R variant demonstrated inhibition of β-sheet structure and, therefore, amyloid formation on the native C-terminal, phenomenon that was associated with functional optimization in calcium and cholesterol management coupled with the optimization of insulin secretion by beta cells. (phoenixpeptide.com)
Functional amyloids play a beneficial role in a variety of physiologic processes (eg, long-term memory formation, gradual release of stored peptide hormones). (medscape.com)