The Purification of Calcium-Binding Protein from the Uterus of the Laying Hen

Fullmer, Curtis S.; Brindak, M. E.; Bär, A.; Wasserman, R. H.

doi:10.3181/00379727-152-39369

Cited by 35 publications

(14 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1, low levels of calcium binding are evident at early stages of development prior to day 12. Between incubation days 12 and 13, however, the activity increases, and it rises rapidly thereafter. The maximal level of calcium binding, which occurs on or about day 19, represents a greater than 10-fold increase over the basal level at day 11. The location of the calciumbinding activity in the CAM was determined by subcellular fractionation (Table 1).…”

Section: Methodsmentioning

confidence: 93%

Calcium-binding protein of chorioallantoic membrane: identification and development expression.

Tuan¹,

Scott²

1977

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

A calcium-binding protein (CaBP) which has a molecular weight of 100,000 and an isoelectric point of 8.0 has been isolated from the chorioallantoic membrane (CAM) of the chick embryo. Expression of the CaBP occurs simultaneously with the onset of calcium absorption from the egg shell by the CAM, and the temporal increase in CaBP activity is coincident with calcium deposition in the embryo. The CAM CaBP differs in properties from the CaBPs of the adult organs, including the vitamin-D-dependent protein of intestine.

show abstract

Section: Methodsmentioning

confidence: 93%

Calcium-binding protein of chorioallantoic membrane: identification and development expression.

Tuan¹,

Scott²

1977

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…CaBP exists as two major forms, a low molecular weight protein of 9 kDa (CaBP-D9k) in the mammalian intestine and a high molecular weight protein of 28 kDa (CaBP-D28k) in the mammalian kidney and brain and avian intestine and shell glands (Fullmer et al, 1976;Parmentier et al, 1987). Their biosynthesis is dependent on circulating levels of the bioactive metabolite of vitamin D, 1,25-dihydroxyvitamin D 3 [1,25(OH) 2 D 3 ] (Taylor, 1981;Bar et al, 1990a,b;Striem and Bar, 1991 the role of CaBP-D28k in chick intestine have been conducted and, accordingly, CaBP-D28k has been shown to be present in all parts of the small intestine in the following sequence: duodenum > jejunum > ileum (Morrissey and Wasserman, 1971).…”

Section: Introductionmentioning

confidence: 99%

Expression and localisation of calbindin D28k in all intestinal segments of the laying hen

Sugiyama

Kikuchi

Hiyama

et al. 2007

British Poultry Science

View full text Add to dashboard Cite

1. The aim of the present study was to investigate expression and localisation of a 28-kDa calcium-binding protein (CaBP-D28k) related to active calcium (Ca) absorption, in the entire intestine of egg-laying hens. 2. Western blotting analysis showed that the entire intestine expressed CaBP-D28k to the following degree: duodenum > jejunum > caecum > ileum > colon. Immunohistochemistry showed strong CaBP-D28k localisation in enterocytes along the villus tip-crypt axis in the duodenum and in villus tips in the caecum and colon. The jejunum and ileum had moderate localisation with respect to the number of immunoreactive cells and staining intensity. 3. These results suggest that laying hens actively absorb Ca in both the large and small intestines.

show abstract

“…Mouse mammary gland therefore resembles epithelial tissues like intestinal mucosa (Wasserman, Corradino, Taylor & Morrissey, 1971), chorioallantoic membrane (Tuan, Scott & Cohn, 1978a) and avian shell gland (Schraer & Schraer, 1971) which transport large amounts of Ca into or out of the plasma compartment. In these tissues Ca transport is hormonally regulated: vitamin D controls transport in intestine and shell gland (Fullmer, Brindak, Bar & Wasserman, 1976) and vitamin K performs this role in the chorioallantoic membrane (Tuan, Scott & Cohn, 1978c). Although it has not been studied in detail in the mammary gland, hormonal control of Ca transport in this tissue is implicit in the observation that the onset of milk secretion at lactogenesis is brought about by the hormonal changes which accompany parturition (Kuhn, 1977).…”

mentioning

confidence: 99%

“…The finding that hormones increase the concentration of an extracellular Ca-binding protein in intestine , avian shell gland Fullmer et al 1976) and chorioallantoic membrane (Tuan, Scott & Cohn, 1978b) has been taken as evidence that a pinocytotic mechanism may be responsible for Ca transport in these tissues Davis, Jones & Hagler, 1979;Tuan et at. 1978b; Terepka, Coleman, Armbrecht & Gunter, 1976).…”

mentioning

confidence: 99%

Calcium fluxes in mouse mammary tissue in vitro: intracellular and extracellular calcium pools

Neville

Peaker

1982

The Journal of Physiology

View full text Add to dashboard Cite

SUMMARY1. The total Ca content of the mammary gland increased from about 2 to 12 #smole/g tissue during the transition from pregnancy to lactation in the mouse.In tissue from lactating mice at least two thirds of the total Ca exchanged with external Ca in 6 hr. There was little non-exchangeable Ca in tissues from pregnant mice.2. At 37 'C the time courses of influx and efflux of 45Ca in lactating tissues could be analysed by assuming three exponential components with rate constants of about 03, 006 and 0005 min-and containing, respectively, 1-7, 1-5 and 4-7 mole 45Ca/g tissue at the steady state.3. The rapidly effluxing component showed the time-and temperature-dependence characteristic of bulk-phase-limited diffusion through the extracellular space. The diffusion coefficient was about one quarter of the self-diffusion coefficient of Ca in aqueous solution, consistent with a tortuosity factor of about 2. A portion of the Ca in this component was displaced by La3+. The amount remaining in the presence of 3 mM-La3+ was close to that expected for free extracellular Ca. The rapid component was therefore interpreted as originating from an extracellular compartment containing both free and bound Ca.4. The rate of efflux of the intermediate component was slowed by a factor of ten when the temperature was decreased from 37 to 0C giving a Q10 of 2-7, expected for membrane transport. The slow component present at 37 'C was not displaced by EGTA or La3+, suggesting that it is not localized extracellularly. It was not apparent in the 0 'C efflux curves. 5. The biphasic time course of uptake of ionophore (A23187)-releasable 45Ca in particulate fractions obtained by homogenization and centrifugation of tissues which had been incubated with the isotope was consistent with the hypothesis that the two slower components of 45Ca flux originate from intracellular compartments. Mitochondrial uptake probably did not contribute significantly to Ca exchange in these tissues.6. 45Calcium fluxes in mammary tissues from pregnant mice also showed three

show abstract

The Purification of Calcium-Binding Protein from the Uterus of the Laying Hen

Cited by 35 publications

References 0 publications

Calcium-binding protein of chorioallantoic membrane: identification and development expression.

Calcium-binding protein of chorioallantoic membrane: identification and development expression.

Expression and localisation of calbindin D28k in all intestinal segments of the laying hen

Calcium fluxes in mouse mammary tissue in vitro: intracellular and extracellular calcium pools

Contact Info

Product

Resources

About