The Distribution of Collagenase in the Rat Uterus During Postpartum Involution: An Immunohistochemical Study

Background: Biogenic amines (BAs) secreted by the sympathetic neural apparatus of rat uterus is reported to be conducive to the uterine functional activity during postpartum involution; the imbalance in BAs ratio could confer postpartum reproductive disorders including improper postpartum involution. Objective: The changes in density of uterine sympathetic nerves implicated in the pathology of endometriosis, adenomyosis, and delayed uterine involution. The present study is aimed to ascertain ‘serotonin’ and ‘catecholamine’ concentrations in mesenteric mast cells (MCs), and structural elements of nerve fibers across the perivascular plexuses (PPs) and single sympathetic nerve terminals (SST). Methods: Furthermore, the density of their spatial distribution (SDP and SDT) in the uterine body, cervix, and mesometrium was determined during postpartum involution. Tissue specimens of postpartum uterus were obtained from 55 nulliparous female Wistar outbred strain rats, which were grouped according to the days after parturition at the time of sacrifice. The nerve fibers of PP and SST exhibited emerald green fluorescence, which was detected by glyoxylic acid fluorescence technique; the fluorescence invoked by BAs was identified by microspectrofluorimetry. Results: Concentrations of BAs were extensive in the varicosities of PP and SST on the 10th day. However, the highest BA concentrations were found in structural elements of PP in the uterine mesometrium in the initial days of postpartum. In mesenteric MC, serotonin and catecholamines were at the highest concentration on 10th day postpartum. Histamines peaked on the 6th day. Conclusion: SDP and SDT were increased significantly in all structural elements of uterine nerve fibers in the uterine body and cervix compared to SDP in mesentery. Considering that catecholamines and serotonin are antagonists in many aspects of their biological action, the ratio of BAs should be well-balanced to maintain anabolic-catabolic equilibrium in the rat uterus.

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Expression of vascular endothelial growth factor receptors and ligands in the rat uterus during the postpartum involution period

Reproductive Biology ◽

10.1016/j.repbio.2013.01.047 ◽

2013 ◽

Vol 13 ◽

pp. 42-43

Author(s):

N. Liman ◽

H. Sağsöz ◽

E. Alan

Keyword(s):

Vascular Endothelial Growth Factor ◽

Growth Factor ◽

Growth Factor Receptors ◽

Vascular Endothelial ◽

Rat Uterus ◽

Postpartum Involution ◽

Endothelial Growth Factor

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Regulation of matrilysin in the rat uterus

Biochemistry and Cell Biology ◽

10.1139/o96-084 ◽

1996 ◽

Vol 74 (6) ◽

pp. 777-784 ◽

Cited By ~ 19

Author(s):

J. Frederick Woessner Jr.

Keyword(s):

Cervical Ripening ◽

Premature Delivery ◽

Prostaglandin E ◽

Rat Uterus ◽

Wide Range ◽

The Matrix ◽

Matrix Metalloproteinase 7 ◽

Postpartum Involution ◽

Last Stage ◽

Natural Inhibitors

Matrilysin was first discovered in the involuting rat uterus; it has also been known as uterine metalloproteinase, putative metalloproteinase (Pump-1), and matrix metalloproteinase 7 (MMP-7). It is the smallest member (28 kDa) of a family of 15 MMPs that together are able to degrade most of the macromolecules of the extracellular matrix. This family is briefly reviewed; all members are zinc metalloproteinases that occur in zymogen form with the active site zinc blocked by cysteine. Matrilysin can degrade a wide range of gelatins, proteoglycans, and glycoproteins of the matrix and can activate several other MMPs including collagenase. With respect to the uterus, matrilysin is localized to epithelial cells and varies in amount with the estrus cycle and is found in high levels during postpartum involution. There is evidence for a role in the last stage of cervical ripening and immediately postpartum. Induction of premature delivery by onapristone and prostaglandin E2advances these changes in matrilysin. Regulation of the enzyme levels in the uterus are considered from four viewpoints: control of protein synthesis (particularly in response to hormones), activation of the proenzyme to functional protease, retention of enzyme by binding to matrix components such as heparan sulfate, and inhibition by natural inhibitors such as tissue inhibitor of metalloproteinases (TIMPs) and α2-macroglobulin.Key words: matrilysin, matrix metalloproteinases, TTMP, uterus, rat uterus.

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PEPTIDYL PEPTIDE HYDROLASES, CATHEPSIN AND COLLAGENASE (?) OF THE RAT UTERUS DURING POSTPARTUM INVOLUTION

Acta Endocrinologica ◽

10.1530/acta.0.0670563 ◽

1971 ◽

Vol 67 (3) ◽

pp. 563-569 ◽

Cited By ~ 3

Author(s):

Dieter Platt ◽

Hanke Frackenpohl

Keyword(s):

Protein Content ◽

Dna Content ◽

Post Partum ◽

Collagenase Activity ◽

Rat Uterus ◽

Cathepsin Activity ◽

Postpartum Involution ◽

Peptide Hydrolases

ABSTRACT 1. The activity of cathepsin and of collagenase in the rat uterus during parturition and in post partum involution increased significantly 60 h after parturition. 2. Cathepsin activity was measured using haemoglobin as substrate at pH 4.1. 3. Collagenase activity was tested with 4-phenyl-azo-benzyloxy-carbonyl-L-prolyl-L-leucyl-glycyl-L-prolyl-D-arginine-OH as substrate at pH 8.5. 4. The protein content of the rat uterus remained constant during post partum involution. 5. The DNA content increased significantly.

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