A trypsin-like enzyme of spermatozoa which is not inhibited by alpha 1 antitrypsin.
Mature male germ cells derived from SPERMATIDS. As spermatids move toward the lumen of the SEMINIFEROUS TUBULES, they undergo extensive structural changes including the loss of cytoplasm, condensation of CHROMATIN into the SPERM HEAD, formation of the ACROSOME cap, the SPERM MIDPIECE and the SPERM TAIL that provides motility.
The cap-like structure covering the anterior portion of SPERM HEAD. Acrosome, derived from LYSOSOMES, is a membrane-bound organelle that contains the required hydrolytic and proteolytic enzymes necessary for sperm penetration of the egg in FERTILIZATION.
Physiologically inactive substances that can be converted to active enzymes.
A tough transparent membrane surrounding the OVUM. It is penetrated by the sperm during FERTILIZATION.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Interactive processes between the oocyte (OVUM) and the sperm (SPERMATOZOA) including sperm adhesion, ACROSOME REACTION, sperm penetration of the ZONA PELLUCIDA, and events leading to FERTILIZATION.

Changes in hyaluronidase, acrosin, and N-acetylhexosaminidase activities of dog sperm after incubation. (1/189)

Hyaluronidase, acrosin and N-acetylhexosaminidase activities were examined in sperm collected from 12 beagle dogs and in culture medium after 0.5 hr and 7 hr of sperm incubation. The activities of the three enzymes were significantly higher at 7 hr than at 0.5 hr (P < 0.05, 0.01), and the increases were associated with sperm capacitation. It was considered that the three enzymes in the dog sperm are related to fertilization by reason of the findings of the release of these enzymes from the sperm into the medium after 7 hr of incubation.  (+info)

Immunolocalization of CRES (Cystatin-related epididymal spermatogenic) protein in the acrosomes of mouse spermatozoa. (2/189)

The CRES (cystatin-related epididymal spermatogenic) protein is a member of the cystatin superfamily of cysteine protease inhibitors and exhibits highly restricted expression in the reproductive tract. We have previously shown that CRES protein is present in elongating spermatids in the testis and is synthesized and secreted by the proximal caput epididymal epithelium. The presence of CRES protein in developing germ cells and in the luminal fluid surrounding maturing spermatozoa prompted us to examine whether CRES protein is associated with spermatozoa. In the studies presented, indirect immunofluorescence, immunogold electron microscopy, and Western blot analysis demonstrated that CRES protein is localized in sperm acrosomes and is released during the acrosome reaction. Interestingly, while the 19- and 14-kDa CRES proteins were present in testicular and proximal caput epididymal spermatozoa, the 14-kDa CRES protein was the predominant form present in mid-caput to cauda epididymal spermatozoa. Furthermore, following the ionophore-induced acrosome reaction, CRES protein localization was similar to that of proacrosin/acrosin in that it was detected in the soluble fraction as well as associated with the acrosome-reacted spermatozoa. The presence of CRES protein in the sperm acrosome, a site of high hydrolytic and proteolytic activity, suggests that CRES may play a role in the regulation of intraacrosomal protein processing or may be involved in fertilization.  (+info)

Effect of recombinant boar beta-acrosin on sperm binding to intact zona pellucida during in vitro fertilization. (3/189)

In a previous paper we demonstrated that boar beta-acrosin recombinant proteins were able to bind non-enzymatically to solubilized pig zona pellucida (ZP) glycoproteins. Here we report the participation of boar beta-acrosin in the secondary binding of sperm to intact pig ZP. This was achieved by using two boar recombinant proteins: beta-acrosin and a mutant of the catalytic site, beta-acrosin Ser/Ala(222). Assays of binding between the iodinated recombinant beta-acrosin and whole ZP showed that this binding could be saturated, was specific, and was stable over time. Using autoradiography, we determined that recombinant beta-acrosin bound on the entire surface of the ZP but initially was distributed heterogeneously. This suggests that the ligands for beta-acrosin may not be homogeneously distributed on the ZP. To study the contribution of acrosin in sperm secondary binding to the ZP, we preincubated in vitro-matured oocytes with these recombinant proteins and then performed in vitro fertilization assays. Under the experimental conditions used, binding of beta-acrosin recombinant proteins did not block sperm penetration. These results suggest that there may be other proteins that participate in the secondary binding, and that these proteins may recognize ligands that are different from those blocked by beta-acrosin recombinant proteins.  (+info)

Tissue-inherent fate of GPI revealed by GPI-anchored GFP transgenesis. (4/189)

To clarify the fate of glycosylphosphatidylinositol (GPI) in mammals, we developed GPI-anchored enhanced green fluorescent protein (EGFP-GPI) and transgenic mice carrying this fusion construct. When it was introduced to culture cells, the EGFP-GPI protein was correctly sorted to plasma membranes and microsomes depending on GPI biosynthesis. Transgenic mice carrying EGFP-GPI were found to show a broad transgene expression. Histologically, a prominent polarized localization of EGFP-GPI protein was observed in various epithelia, the nervous system and liver and secreted from some exocrine glands, as well as non-polarized presence in non-epithelial tissues, demonstrating a tissue-inherent manner of GPI sorting.  (+info)

Expression of human proacrosin in Escherichia coli and binding to zona pellucida. (5/189)

Proacrosin is a multifunctional protein present in the sperm acrosome. This study characterizes the expression of human proacrosin in bacteria and assesses zona pellucida binding activity. The cDNA encoding human proacrosin was subcloned in pGEX-3X and pET-22b vectors. In the pGEX system, expression of the full-length fusion protein was not detected. In the pET system, an expression product with an apparent molecular size similar to that expected for the proenzyme (Rec-40, 42-44 kDa) was recognized by a monoclonal antibody to human acrosin, AcrC5F10. A 32-34-kDa protein (Rec-30), not recognized by AcrC5F10 on Western blots, was the major expression product. Proteins of 21 (Rec-20) and 18 (Rec-10) kDa were recovered as insoluble expression products as were Rec-40 and Rec-30, and truncated products from the C terminus were detected in the soluble fraction. Rec-40 and Rec-30 coexisted at any culture time tested. Immune serum raised against Rec-30 (AntiRec-30) stained the acrosomal region of permeabilized human spermatozoa and recognized the recombinant proteins and proacrosin from human sperm extracts. Amino acid sequence analysis indicated that Rec-30, Rec-20, and Rec-10 are N-terminal fragments of proacrosin. The recombinant proteins Rec-40, -30, -20, and -10 were found to interact with homologous (125)I-zona pellucida glycoproteins.  (+info)

The Golgi apparatus segregates from the lysosomal/acrosomal vesicle during rhesus spermiogenesis: structural alterations. (6/189)

The acrosome is an acidic secretory vesicle containing hydrolytic enzymes that are involved in the sperm's passage across the zona pellucida. Imaging of the acrosomal vesicle and the Golgi apparatus in live rhesus monkey spermatids was accomplished by using the vital fluorescent probe LysoTracker DND-26. Concurrently, the dynamics of living spermatid mitochondria was visualized using the specific probe MitoTracker CMTRos and LysoTracker DND-26 detected the acrosomal vesicle from its formation through spermatid differentiation. LysoTracker DND-26 also labeled the Golgi apparatus in spermatogenic cells. In spermatocytes the Golgi is spherical and, in round spermatids, it is localized over the acrosomal vesicle, as confirmed by using polyclonal antibodies against Golgin-95/GM130, Golgin-97, and Golgin-160. Using both live LysoTracker DND-26 imaging and Golgi antibodies, we found that the Golgi apparatus is cast off from the acrosomal vesicle and migrates toward the sperm tail in elongated spermatids. The Golgi is discarded in the cytoplasmic droplet and is undetectable in mature ejaculated spermatozoa. The combined utilization of three vital fluorescent probes (Hoechst 33342, LysoTracker DND-26, and MitoTracker CMTRos) permits the dynamic imaging of four organelles during primate spermiogenesis: the nucleus, the mitochondria, the acrosomal vesicle, and the Golgi apparatus.  (+info)

A basic 18-amino acid peptide contains the polysulfate-binding domain responsible for activation of the boar proacrosin/acrosin system. (7/189)

Proacrosin is the zymogen of acrosin, a serine protease localized in the acrosomal matrix of mammalian sperm. Proacrosin/acrosin binds to solubilized zona pellucida glycoproteins (ZPGs) and various polysulfates in a non-enzymatic mechanism. In addition, both polysulfates and ZPGs induce proacrosin activation once they bind to the polysulfate-binding domain (PSBD) of the enzyme. We show here that the peptide (43)IFMYHNNRRYHTCGGILL(60) inhibited the proacrosin activation induced by either fucoidan or ZPGs. In addition, the peptide was recognized by the monoclonal antibody C5F10, which is directed against the PSBD region. Our data suggest that the PSBD is composed of many "subsites" that may or may not interact with each other.  (+info)

Trypsin/acrosin inhibitor activity of rat and guinea pig caltrin proteins. Structural and functional studies. (8/189)

Dramatic inhibition of trypsin activity by rat caltrin and guinea pig caltrin I was spectrophotometrically demonstrated using the artificial substrate benzoylarginyl ethyl ester. Approximately 6% and 21% of residual proteolytic activity was recorded after preincubating the enzyme with 0.22 and 0.27 microM rat caltrin and guinea pig caltrin I, respectively. Reduction and carboxymethylation of the cysteine residues abolished the inhibitor activity of both caltrin proteins. Rat caltrin and guinea pig caltrin I show structural homology with secretory trypsin/acrosin inhibitor proteins isolated from boar and human seminal plasma and mouse seminal vesicle secretion and share a fragment of 13 amino acids of almost identical sequence (DPVCGTDGH/K/ITYG/AN), which is also present in the structure of Kazal-type trypsin inhibitor proteins from different mammalian tissues. Bovine, mouse, and guinea pig caltrin II, three caltrin proteins that have no structural homology with rat caltrin or guinea pig caltrin I, lack trypsin inhibitor activity. Rat caltrin, guinea pig caltrin I, and the mouse seminal vesicle trypsin inhibitor protein P12, which also inhibits Ca(2+) uptake into epididymal spermatozoa (mouse caltrin I), bound specifically to the sperm head, on the acrosomal region, as detected by indirect immunofluorescence. They also inhibited the acrosin activity in the gelatin film assay. Caltrin I may play an important role in the control of sperm functions such as Ca(2+) influx in the acrosome reaction and activation of acrosin and other serine-proteases at the proper site and proper time to ensure successful fertilization.  (+info)

Acrosin is a proteolytic enzyme that is found in the acrosome, which is a cap-like structure located on the anterior part of the sperm head. This enzyme plays an essential role in the fertilization process by helping the sperm to penetrate the zona pellucida, which is the glycoprotein coat surrounding the egg.

Acrosin is released from the acrosome when the sperm encounters the zona pellucida, and it begins to digest the glycoproteins in the zona pellucida, creating a path for the sperm to reach and fuse with the egg's plasma membrane. This enzyme is synthesized and stored in the acrosome during spermatogenesis and is activated during the acrosome reaction, which is a critical event in fertilization.

Defects in acrosin function or regulation have been implicated in male infertility, making it an important area of research in reproductive biology.

Spermatozoa are the male reproductive cells, or gametes, that are produced in the testes. They are microscopic, flagellated (tail-equipped) cells that are highly specialized for fertilization. A spermatozoon consists of a head, neck, and tail. The head contains the genetic material within the nucleus, covered by a cap-like structure called the acrosome which contains enzymes to help the sperm penetrate the female's egg (ovum). The long, thin tail propels the sperm forward through fluid, such as semen, enabling its journey towards the egg for fertilization.

The acrosome is a specialized structure located on the anterior part of the sperm head in many species of animals, including humans. It contains enzymes that help the sperm penetrate the outer covering of the egg (zona pellucida) during fertilization. The acrosome reaction is the process by which the acrosome releases its enzymes, allowing the sperm to digest a path through the zona pellucida and reach the egg plasma membrane for fusion and fertilization.

The acrosome is formed during spermatogenesis, the process of sperm production in the testis, from the Golgi apparatus, a cellular organelle involved in protein trafficking and modification. The acrosome contains hydrolytic enzymes such as hyaluronidase, acrosin, and proteases that are activated during the acrosome reaction to facilitate sperm-egg fusion.

Abnormalities in acrosome formation or function can lead to infertility in males.

Enzyme precursors are typically referred to as zymogens or proenzymes. These are inactive forms of enzymes that can be activated under specific conditions. When the need for the enzyme's function arises, the proenzyme is converted into its active form through a process called proteolysis, where it is cleaved by another enzyme. This mechanism helps control and regulate the activation of certain enzymes in the body, preventing unwanted or premature reactions. A well-known example of an enzyme precursor is trypsinogen, which is converted into its active form, trypsin, in the digestive system.

Zona pellucida is a term used in the field of reproductive biology and it refers to the glycoprotein membrane that surrounds mammalian oocytes (immature egg cells). This membrane plays a crucial role in the fertilization process. It has receptors for sperm, and upon binding with the sperm, it undergoes changes that prevent other sperm from entering, a process known as the zona reaction. This membrane is also involved in the early development of the embryo.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Sperm-ovum interactions, also known as sperm-egg interactions, refer to the specific series of events that occur between a spermatozoon (sperm) and an oocyte (egg or ovum) during fertilization in sexual reproduction.

The process begins with the sperm's attachment to the zona pellucida, a glycoprotein layer surrounding the oocyte. This interaction is mediated by specific proteins on the surface of both the sperm and the zona pellucida. Following attachment, the sperm undergoes the acrosome reaction, during which enzymes are released from the sperm's head to help digest and penetrate the zona pellucida.

Once the sperm has successfully traversed the zona pellucida, it makes contact with the oocyte's plasma membrane, triggering the fusion of the sperm and egg membranes. This results in the release of the sperm's genetic material into the oocyte's cytoplasm and the initiation of a series of intracellular signaling events within the oocyte that ultimately lead to its completion of meiosis II and formation of a zygote, marking the beginning of embryonic development.

Proper sperm-ovum interactions are crucial for successful fertilization and subsequent embryonic development, and any disruptions in these processes can result in infertility or early pregnancy loss.

Acrosin is a digestive enzyme that acts as a protease. In humans, acrosin is encoded by the ACR gene. Acrosin is released from ... the high concentrations of PCI would inhibit acrosin from inflicting proteolytic damage on nearby tissues. β-acrosin ... Acrosin is the major proteinase present in the acrosome of mature spermatozoa. It is stored in the acrosome in its precursor ... Acrosin regulation has been found to occur through protein C inhibitor (PCI). PCI is present in the male reproductive tract at ...
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Where is acrosin found?. acrosome. Acrosin is the major proteinase present in the acrosome of mature spermatozoa. It is stored ... Is acrosin a druggable target for contraception?. Acrosin may represent as a uniquely druggable target due to its location and ... The sperm enzyme acrosin functions in sperm binding to, and penetration of, the egg zona pellucida. Acrosin is a three domain ... Is acrosin a protease?. Acrosin (a typical serine protease) functions during fertilization in several significant ways which ...
enables acrosin binding IBA Inferred from Biological aspect of Ancestor. more info ...
Serine peptidase inhibitor, Kazal Type II (acrosin-trypsin inhibitor). Chemokine (C-C motif) ligand 27 ...
acrosin. -. 3.4.21.100. sedolisin. -. 3.4.21.101. xanthomonalisin. -. 3.4.21.102. C-terminal processing peptidase. -. ...
Acrosin - Prolyl endopeptidase - Pronase - Proprotein convertases (1, 2) - Subtilisin/Furin - Streptokinase - S1P. ...
The compound inhibits hyaluronidase and acrosin, induces sperm acrosomal loss, and is contraceptive in the rabbit model. ...
Acrosin (1) Actin (muscle) (1) Ag85b (M. tuberculosis) (1) AGPS (1) AGR2/AGR3 (1) ...
Acrosin (1) Actin (muscle) (1) Ag85b (M. tuberculosis) (1) AGPS (2) AGR2/AGR3 (1) ...
PRSS8 shares sequence homology at the amino acid level with acrosin, plasma kallikrein, hepsin, testisin and gamma tryptase.. [ ...
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O Decreased acrosin in sperm head,O Decreased activity of 3-hydroxyacyl-CoA dehydrogenase,O Decreased activity of NADPH oxidase ...
Description: A sandwich ELISA for quantitative measurement of Human Anti acrosin antibodies in samples from blood, plasma, ...
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In mammals, it contains acrosomin made of hyaluronidase and acrosin (zona lysin). ...
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