Linked Life Data

9828198

Source:http://linkedlifedata.com/resource/pubmed/id/9828198

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-12-28
pubmed:abstractText
We examined the developmental profile of a kazal-type trypsin inhibitor (P12) of Mr 6126 in mouse seminal vesicle, characterized its binding sites on the surface of sperm, and assessed its effect on Ca2+ uptake by spermatozoa. Among the genital tracts of adult mice, P12 was found only in the male accessory glands including seminal vesicle, coagulating gland, and prostate. It was immunolocalized on the luminal epithelium of the primary and secondary folds in both the seminal vesicle and coagulating gland, and on the folds projecting into the lumen of the glandular alveolus in the prostate. The protein and its RNA message in seminal vesicle did not appear in the prepubertal period, but expression coincided with maturation. Castration of adult mice resulted in cessation of P12 expression. Treatment of the castrated mice with testosterone propionate in corn oil restored the protein expression in the seminal vesicle. Spermatozoa collected from caudal epididymis were devoid of P12. Cytochemical study illustrated a P12-binding region on the anterior acrosomes of cells preincubated with P12. Analysis of equilibrium data from the binding assay using 125I-P12 with a Scatchard plot showed a single type of P12-binding sites on sperm, with an apparent dissociation constant of 70.15 +/- 5.25 nM and the capacity of 1.49 +/- 0.06 x 10(6) binding sites/cell. The protein could serve as a calcium transport inhibitor to suppress a great extent of Ca2+ uptake by spermatozoa. The immunohistochemical staining patterns of testis revealed that the P12-binding sites appeared on postmeiotic cells such as spermatids and spermatozoa, but were absent in Leydig cells, Sertoli cells, spermatogonia, and spermatocytes in seminiferous tubules.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-3363
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1498-505
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9828198-Animals, pubmed-meshheading:9828198-Binding Sites, pubmed-meshheading:9828198-Biological Transport, pubmed-meshheading:9828198-Blotting, Western, pubmed-meshheading:9828198-Calcium, pubmed-meshheading:9828198-DNA-Binding Proteins, pubmed-meshheading:9828198-Gene Expression, pubmed-meshheading:9828198-Genitalia, Male, pubmed-meshheading:9828198-Glycoproteins, pubmed-meshheading:9828198-Immunohistochemistry, pubmed-meshheading:9828198-Male, pubmed-meshheading:9828198-Mice, pubmed-meshheading:9828198-Mice, Inbred ICR, pubmed-meshheading:9828198-Prostatic Secretory Proteins, pubmed-meshheading:9828198-Proteins, pubmed-meshheading:9828198-RNA, Messenger, pubmed-meshheading:9828198-Recombinant Proteins, pubmed-meshheading:9828198-Seminal Plasma Proteins, pubmed-meshheading:9828198-Seminal Vesicles, pubmed-meshheading:9828198-Sexual Maturation, pubmed-meshheading:9828198-Sperm Capacitation, pubmed-meshheading:9828198-Spermatozoa, pubmed-meshheading:9828198-Tissue Distribution
pubmed:year
1998
pubmed:articleTitle
Developmental profile of a caltrin-like protease inhibitor, P12, in mouse seminal vesicle and characterization of its binding sites on sperm surface.
pubmed:affiliation
Institute of Biochemical Sciences, College of Science, National Taiwan University, and.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't