Biochemcial Characterization of the Mouse Testis Trypsin-like protein, TSP36
Autor: | Chung-Mao Ou, 歐宗茂 |
---|---|
Rok vydání: | 2002 |
Druh dokumentu: | 學位論文 ; thesis |
Popis: | 90 MSVS TI (P12), a kazal-type trypsin inhibitor, has been demonstrated by our research group to play an important role in mouse reproduction. Dr. Jinn of our group had utilized yeast two hybrid system to fish the potential candidates that may associate with P12 in the cDNA library of mouse testis. One of them showed a high homology to testis specific serine protease (TESP), such as TESP2 and TESP4 reported thus far.The genome structure of 7412 bp in this gene (TSP 36), including 939 bp in the 5’-flanking region, 6 exons and 5 introns. This gene encodes a protein with 317 amino acids that sum to give a molecular mass of 35,722 Da. As compared to trypsin-like protease that have conserved Histidine, Aspartic acid and Serine for the catalytic lysis of a peptide bond and have a conserved Aspartic acid for the substrate binding. The corresponding active serine is absent but substituted by proline in TSP36. Among the male and female reproductive tracts, TSP36 gene was the exclusive expression in testis and had a positive correlation of TSP36 RNA expression to the developmental profile of mouse testis. This may suggest that the androgen-stimulated TSP36 is expressing in testis. In fact, there are 9 nucleotide segments with 50-75% similarity to the consensus sequence of androgen response element in the TSP36 gene. The results of histochemical study revealed the presence of TSP36 in secondary spermatocyte, spermatid and mature spermatozoa of seminiferous tubules. Moreover, TSP36 was immunodetected on the tail of mouse sperm. |
Databáze: | Networked Digital Library of Theses & Dissertations |
Externí odkaz: |