Increased Collagenase Activity is not Detectable in Cervical Softening in the Ewe

John G. Raynes , John C. Anderson , R.J. Fitzpatrick , Hilary Dobson
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引用次数: 9

Abstract

Cervical tissue from ewes at various stages of pregnancy was examined for evidence that collagenase is involved in the process of cervical softening. Collagenase activity was detected in medium after 2–3 days culture of ovine cervical explants, but there was no significant difference in total enzymic activity produced by explants from non-pregnant, early pregnant or late pregnant animals when expressed as units/mg wet weight of tissue over five days in culture. Oestradiol infusion into ewes prior to parturition did not alter the enzyme activity subsequently produced in explant culture. However, the DNA concentration, and hence the number of cells per unit volume, decreased significantly with length of pregnancy, this effect being due to expansion of cervical tissue which occurs late in pregnancy. Thus, if collagenase activity is expressed relative to DNA and hence cell number, there is evidence for increased production per cell in order to keep the tissue concentration constant. However, as the concentration of collagen in cervix remains constant during pregnancy, the ratio of collagenase activity to collagen is also constant. It is therefore concluded that there is no evidence of a role for increased collagenase activity in cervical softening in the ewe.

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在母羊的颈椎软化中没有检测到胶原酶活性的增加
从母羊在怀孕的各个阶段宫颈组织检查的证据,胶原酶是参与颈椎软化的过程。在培养2-3天后,在培养基中检测到胶原酶活性,但在培养5天后,以单位/mg组织湿重表示,未怀孕、怀孕早期和怀孕晚期动物的外植体产生的总酶活性没有显著差异。母羊在分娩前输注雌二醇并没有改变随后在外植体培养中产生的酶活性。然而,DNA浓度以及单位体积的细胞数量随着妊娠时间的延长而显著下降,这种影响是由于妊娠后期宫颈组织的扩张造成的。因此,如果胶原酶活性相对于DNA和细胞数量表达,则有证据表明,为了保持组织浓度恒定,每个细胞的产量会增加。然而,由于怀孕期间子宫颈内胶原蛋白的浓度保持不变,胶原酶活性与胶原蛋白的比值也保持不变。因此,没有证据表明胶原酶活性的增加在母羊颈椎软化中起作用。
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Increased Collagenase Activity is not Detectable in Cervical Softening in the Ewe Abstracts From The Second International Conference On Molecular Biology And Pathology Of Matrix' Philadelphia, Pennsylvania, June 15-18,1988 Authors Index The Drosophila Homoeotic Gene Spalt is Structurally Related to Collagen αl(IV) Chain Quantitation of Collagen Fragments and Gelatin by Deconvolution of Polarimetry Denaturation Curves
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