عنوان
پدید آورنده
موضوع
رده
کتابخانه
محل استقرار
شماره کتابشناسی ملی
شماره
TLpq230836495
زبان اثر
زبان متن نوشتاري يا گفتاري و مانند آن
انگلیسی
عنوان و نام پديدآور
عنوان اصلي
Biochemical mechanism and hormonal regulation of dilatation of the uterine cervix at parturition
نام عام مواد
[Thesis]
نام نخستين پديدآور
M. R. Rajabi
وضعیت نشر و پخش و غیره
نام ناشر، پخش کننده و غيره
McGill University (Canada)
تاریخ نشرو بخش و غیره
1990
مشخصات ظاهری
نام خاص و کميت اثر
218
یادداشتهای مربوط به پایان نامه ها
جزئيات پايان نامه و نوع درجه آن
Ph.D.
کسي که مدرک را اعطا کرده
McGill University (Canada)
امتياز متن
1990
یادداشتهای مربوط به خلاصه یا چکیده
متن يادداشت
Studies were designed to investigate the biochemical mechanism and hormonal regulation of dilatation of the uterine cervix at parturition. The suitability of the guinea pig animal model was established by demonstrating collagenolysis in the uterine cervix similar to the changes reported in women by light and electron microscopy. By 50 days gestation, there was a 50% decrease in collagen content in the cervix. At parturition (68 2 days) there was a 6-fold increase in procollagenase, a 26-fold increase in the tissue inhibitor of metalloproteinase (TIMP) and a 2-fold increase in net collagenase activity in cervical extracts. Cervices in organ culture obtained at birth produced 2.9 times more procollagenase, 1.6 times more TIMP and a 10-fold increase in net collagenase activity when compared to nonpregnant or 25 days pregnant animals. Estradiol stimulated the production of procollagenase, TIMP and net collagenase activity in cervical organ cultures. Using primary monolayer cervical cell cultures derived from 50 day pregnant guinea pigs, procollagenase enzyme and its mRNA were stimulated up to 2-fold by recombinant human interleukin 1usd\betausd (IL-1usd\betausd), estrogens and progesterone. Procollagenase production was completely abolished by cycloheximide and by actinomycin D indicating the need for translation and transcription respectively. The mechanism of signal transduction of procollagenase was also investigated. A rabbit polyclonal antiserum (R4718) that specifically reacts with epitopes on denatured and degraded usd\alphausd2 chain of guinea pig type I collagen was used to demonstrate degradation of type I collagen in the extracellular matrix of the dilated cervix at parturition. Physiological concentrations of 17usd\betausd-estradiol stimulated degradation of type I collagen in the nonpregnant cervix in organ culture. This effect was completely blocked by progesterone (100 muM). These studies indicate that cervical dilatation at parturition involves estrogen-induced, collagenase-mediated degradation of type I collagen through a prostaglandin intermediate and activation of protein kinase C.
موضوع (اسم عام یاعبارت اسمی عام)
موضوع مستند نشده
Anatomy & physiology
موضوع مستند نشده
Anatomy & physiology
موضوع مستند نشده
Animals
موضوع مستند نشده
Biochemistry
موضوع مستند نشده
Biological sciences
موضوع مستند نشده
Pure sciences
نام شخص به منزله سر شناسه - (مسئولیت معنوی درجه اول )
مستند نام اشخاص تاييد نشده
M. R. Rajabi
دسترسی و محل الکترونیکی
نام الکترونيکي
مطالعه متن کتاب وضعیت انتشار
فرمت انتشار
p
اطلاعات رکورد کتابشناسی
نوع ماده
[Thesis]
کد کاربرگه
276903
اطلاعات دسترسی رکورد
سطح دسترسي
a
تكميل شده
Y
