Ca2+-activated proteinase in the rat. Quantification by immunoassay in the uterus during pregnancy and involution, and in other tissues

Elce, John S.; Baenziger, J E; Young, Dorothy C.

doi:10.1042/bj2200507

Cited by 13 publications

(12 citation statements)

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“…It would be of interest, therefore, to know how the synthesis of calpain is regulated. We have previously made some measurements of calpain in the pregnant rat uterus by means of a sandwich e.l.i.s.a., with results indicating a disproportionate increase in calpain activity during pregnancy [13]. These results led us to investigate the regulation of calpain synthesis during pregnancy, measuring calpain protein by immunochemical means and mRNA by means of nucleic acid probes that we have recently isolated for the calpains.…”

Section: Introductionmentioning

confidence: 94%

“…We had measured calpain previously in the uterus by means of a sandwich e.l.i.s.a. with '25I-labelled anticalpain IgG, and reported a marked increase in calpain in pregnancy with respect to wet weight [13]. Further work led us to doubt these results, and we devoted much effort to development of a classical radioimmunoassay, and of a competitive e.l.i.s.a.…”

Section: Immunoblotting Of Calpainmentioning

confidence: 99%

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Constitutive expression of calpain II in the rat uterus during pregnancy and involution

Samis

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Graham

et al. 1991

Biochemical Journal

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Partial genomic clones for the 80 kDa subunits of rat calpains I and II have been isolated. Some exons have been located and sequenced, and used to synthesize RNA probes specific for each isoenzyme. The levels of total DNA, soluble protein, calpain II 80 kDa subunit and the mRNA for this subunit were measured in parallel in separate extracts of non-pregnant, pregnant and post-partum rat uteri. The amount of total DNA, expressed as mg/g wet wt. of tissue, was found to remain constant throughout this period, except for a slight rise during involution. Calpain I was present in all samples in very small amounts. The amounts of calpain II 80 kDa subunit (measured on immunoblots) and of its mRNA (measured by means of slot-blots) also did not vary, when expressed in terms of units per g wet wt., during the 10-fold growth of the uterus during pregnancy and its post-partum involution. It was concluded that expression of calpain II was constitutive in this normal tissue, which is undergoing rapid growth and involution under complex hormonal control.

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Section: Introductionmentioning

confidence: 94%

Section: Immunoblotting Of Calpainmentioning

confidence: 99%

Constitutive expression of calpain II in the rat uterus during pregnancy and involution

Samis

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Graham

et al. 1991

Biochemical Journal

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“…); however, their physiological function(s) in vivo is currently unknown. Several research groups have attempted to measure tissue CDP activities during altered conditions of protein metabolism (Dayton et al, 1979;Brooks et al, 1983;Elce et al, 1984) to gain an understanding of their physiological role. However, it is difficult to measure Ca2+-dependent proteolytic activity in tissue extracts quantitatively, because the CDP inhibitor is also cytoplasmic and can specifically interact with either CDP I or CDP II (Murachi, 1983;.…”

Section: Introductionmentioning

confidence: 99%

“…2-100 mg tissue samples). Immunoassays have also been used to measure Ca2+-dependent proteinases (Elce et al, 1983(Elce et al, , 1984. Although these immunoassays require only small amounts of tissue, they do not directly measure CDP activity and may not allow discrimination between CDP I and CDP II.…”

Section: Introductionmentioning

confidence: 99%

Fractionation and quantification of calcium-dependent proteinase activity from small tissue samples

Clark¹,

DeMartino²,

Croall³

1986

Biochemical Journal

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Almost all mammalian tissues contain a cytoplasmic Ca2+-dependent proteolytic system consisting of two different proteinases (CDP I and CDP II) and an endogenous inhibitor specific for these proteinases. It was difficult to determine the relative activities of CDP I and CDP II directly and accurately without extensive purification, requiring relatively large amounts of tissue. We developed a simple technique based on Reactive Red-agarose affinity chromatography for quantitatively measuring CDP II activities in small (less than 100 mg) tissue samples. This technique is rapid, sensitive and highly reproducible. CDP II activities can be quantified in numerous tissue samples in a single day. Using this method, we analysed the components of the CDP system in various rat tissues and demonstrated quantitative differences in CDP II activities as well as relative differences in the amounts of CDP-inhibitor activity among the various tissues. This technique should prove useful in the efforts to define the currently unknown physiological function(s) of the Ca2+-dependent proteolytic system by allowing comparison of CDP activities in tissues under diverse conditions of protein metabolism.

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“…According to these studies, the presence of calpain-1, calpain-2, and calpastatin, which is endogen specific inhibitor of these calpains, was reported in human endometrial cancer type (Salehin et al, 2010). Furthermore, it has been reported that calpain-2 is expressed constitutively in the rat uterus during pregnancy and postpartum involution (Samis et al, 1991) and the Ca21-activated proteinase may have some role in tissue resorption during uterine involution (Elce et al, 1984). Apoptosis is tightly regulated by a fine-tuned balance between proapoptotic and antiapoptotic factors.…”

Section: Introductionmentioning

confidence: 99%

Involution dependent changes in distribution and localization of bax, survivin, caspase‐3, and calpain‐1 in the rat endometrium

Alan

Lïman

2016

Microscopy Res & Technique

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The endometrial layer of the uterus is characterized by continuous cycle of cell growth and apoptosis in response to hormonal changes. Apoptosis is regulated by several apoptotic regulators, but their significance in involuting uterus has not been well understood. For that reason, aim of this study was to investigate possible role of apoptosis-related proteins (bax and survivin) and enzymes (caspase-3 and calpain-1) in the involuting uterus of the rat, using immunohistochemistry. Our results indicated cytoplasmic and nuclear immunostaining for bax, caspase-3, calpain-1 and survivin proteins were found in the endometrial epithelium and stromal cells such as fibroblasts, mast cells and macrophages, and blood vessels; however, calpain-1 immunoreactivity in the endometrial fibroblast was quite weak or absent. Supranuclear punctate bax immunolabelling was also observed in the endometrial fibroblasts and luminal and glandular epithelial cells from days 1st and 3rd following parturition, respectively. Although survivin was localized in the apical cytoplasm underneath the apical membrane of the luminal epithelium on the 1st and 3rd days, it was also localized in the apicolateral membrane and basal cytoplasm on the 10th and 15th days of involution. Immunostainigs demonstrated that expression patterns of all examined proteins varied with structural changes in the luminal epithelium, and number of immunopositive fibroblasts for bax, caspase-3 and survivin increased with advance of postpartum days and reached a maximum on postpartum days 10 and 15. These results suggest that the process of postpartum involution of endometrium may be regulated by apoptotic and non-apoptotic activity of bax, caspase-3, calpain-1, and survivin.

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Ca2+-activated proteinase in the rat. Quantification by immunoassay in the uterus during pregnancy and involution, and in other tissues

Cited by 13 publications

References 44 publications

Constitutive expression of calpain II in the rat uterus during pregnancy and involution

Constitutive expression of calpain II in the rat uterus during pregnancy and involution

Fractionation and quantification of calcium-dependent proteinase activity from small tissue samples

Involution dependent changes in distribution and localization of bax, survivin, caspase‐3, and calpain‐1 in the rat endometrium

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