Demonstration of two different vitamin D-dependent calcium-binding proteins in rat intestinal mucosa.

Moriuchi, Sachiko; Yamanouchi, Toshikazu; Hosoya, Norimasa

doi:10.3177/jnsv.21.251

Cited by 18 publications

(6 citation statements)

References 6 publications

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“…A similar vitamin D dependency of S-CaBP in rat duodenum [Drescher and DeLuca, 1971;Moriuchi et al, 1975;Thomasset et al. 1979a, b] has also been demonstrated.…”

Section: Discussionmentioning

confidence: 91%

“…One of these (L-CaBP) has a molecular weight of 28.000 and seems to resemble the chick D-CaBP mentioned above, and has been isolated from rat kidney [Hermsdorf and Bronner, 1975], human kidney [Piazolo et al, 1971;Morrissey and Rath, 1974], and dog kidney [Sands and Kessler, 1971], as well as from human brain [Baimbridge et al, 1980], The antisera raised against L-CaBP from human kidney react against D-CaBP from chick duodenum [Morrissey et al, 1975[Morrissey et al, , 1978a and the antiserum raised against chick duodenal D-CaBP gives immuno-chemical staining in chick brain [Roth et al, 1981] and rat brain [Jamie et al, 1981b] and also rat kidney [Rhoten and Christakos, 1981]. The second mammalian vitamin D-dependent CaBP (S-CaBP) has a smaller molecular weight (9.000) and has been isolated from rat and pig intestinal mu cosa [Hitchman and Harrison, 1972;Moriuchi et al, 1975] where it predominates in the duodenum, and it has been detected by RIA in many other organs of the pig Murray et al, 1974Murray et al, . 1975, Using antiserum raised against chick D-CaBP, the cellular localization of this protein has been described by immunohisto chemical techniques in many organs of chick [Lipiello and Wasserman, 1975;Taylor, 1981;Jande et al.…”

Section: Introductionmentioning

confidence: 99%

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Immunocytochemical Demonstration of Two Vitamin D-Dependent Calcium-Binding Proteins in Mammalian Kidney

Schreiner

Jande

Parkes

et al. 1983

Cells Tissues Organs

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Distribution of vitamin D-dependent calcium-binding proteins (CaBPs) were studied in four mammalian species using monospecific antibodies raised against chick duodenal CaBP (D-CaBP), human cerebellar CaBP (L-CaBP), and rat duodenal CaBP (S-CaBP). The immunoperoxidase technique of unlabelled antibodies was employed. The distribution of D-CaBP/L-CaBP was identical in all the species studied except for the monkey, in the rat, pig, and human nephrons, D-CaBP/L-CaBP was seen in the cytoplasm of the cells of the distal convoluted tubules, initial segments of the collecting ducts and interspersed cells of the collecting ducts. Proximal convoluted tubules, glomeruli and maculae densae were negative. In the monkey, in addition to the cells of the distal convoluted tubules, the cells along the entire length of the collecting ducts were also strongly positive. S-CaBP was found to be species-specific, and hence positive results were obtained only in the rat nephron. The strongest positive reaction for S-CaBP was seen in the cells of the distal convoluted tubules. These same cells were also positive for D-CaBP/L-CaBP. S-CaBP was also detected in the cells of the thick ascending limb of the loop of Henle, along the entire length of the collecting ducts and in smaller amounts in cells of the macula densa. Intracellularly the S-CaBP was present only in the apical cytoplasm of positive cells. D-CaBP/L-CaBP stained the entire cytoplasm but the staining in the apical cytoplasm was denser.

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“…A similar vitamin D dependency of S-CaBP in rat duodenum [Drescher and DeLuca, 1971;Moriuchi et al, 1975;Thomasset et al. 1979a, b] has also been demonstrated.…”

Section: Discussionmentioning

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Immunocytochemical Demonstration of Two Vitamin D-Dependent Calcium-Binding Proteins in Mammalian Kidney

Schreiner

Jande

Parkes

et al. 1983

Cells Tissues Organs

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“…Indeed, the presence of small amounts of this protein in rat and mouse duodenum has been reported [6,25,39]. Indeed, the presence of small amounts of this protein in rat and mouse duodenum has been reported [6,25,39].…”

Section: Introductionmentioning

confidence: 98%

Calbindin‐D_28K and the peptidergic neuroendocrine system in rat gut: an immunohistochemical study

Résibois

Vienne

Pochet

1988

Biology of the Cell

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Calbindin-D28K was immunohistochemically localized in myenteric and submucosal plexuses throughout the rat intestine. Calbindin-D28K immunoreactivity was found in about half of myenteric neurons and in more than 90% of submucosal neurons. Calbindin-D28K was also observed in nerve processes running inside ganglia, muscle layers and lamina propria. No correlation could be established between the presence of calbindin-D28K and the distribution of neuropeptides localized in this study (VIP, enkephalin, somatostatin and substance P). In addition, some endocrine-like cells of the ileum were calbindin-D28K-positive. Half of these endocrine cells also contained neurotensin but none of the other neuropeptides investigated.

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“…CaBP was prepared from pooled mucosa (Moriuchi et al, 1975) with .005% Thimerosal in the buffer. Also of interest was any similarity between the serum CaBP(s), phosvitin, and the CaBP of the uterus and duodenum.…”

Section: Introductionmentioning

confidence: 99%

“…Calcium binding to proteins was measured by gel filtration on Sephadex G-200 columns using a 4S Ca buffer (Moriuchi et al, 1975). Calcium binding to proteins was measured by gel filtration on Sephadex G-200 columns using a 4S Ca buffer (Moriuchi et al, 1975).…”

Section: Introductionmentioning

confidence: 99%

Calcium-Binding Proteins in Serum of Chickens: Vitellogenin and Albumin

et al. 1980

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The Ca-binding proteins of hen serum were resolved by gel filtration in 45Ca buffer and were named CaBP(1) and CaBP(2). The major calcium-binding protein, CaBP(1), had a molecular size of 6.0 X 10(5) daltons and appears to be vitellogenin. Deeley et al. (1975) described vitellogenin as the precursor of lipovitellin and phosvitin, the Ca-binding proteins of egg yolk. The present paper demonstrates that "native" vitellogenin is a calcium-binding protein in the serum of laying chickens. The CaBP(2) co-eluted with and was immunologically identical to chicken serum albumin which also bound 45Ca. Data from elution profiles and phosphorus assays indicated that CaBP(1) and CaBP(2) were different from phosvitin and the Ca-binding proteins of the duodenum and uterus.

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Demonstration of two different vitamin D-dependent calcium-binding proteins in rat intestinal mucosa.

Cited by 18 publications

References 6 publications

Immunocytochemical Demonstration of Two Vitamin D-Dependent Calcium-Binding Proteins in Mammalian Kidney

Immunocytochemical Demonstration of Two Vitamin D-Dependent Calcium-Binding Proteins in Mammalian Kidney

Calbindin‐D_28K and the peptidergic neuroendocrine system in rat gut: an immunohistochemical study

Calcium-Binding Proteins in Serum of Chickens: Vitellogenin and Albumin

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Demonstration of two different vitamin D-dependent calcium-binding proteins in rat intestinal mucosa.

Cited by 18 publications

References 6 publications

Immunocytochemical Demonstration of Two Vitamin D-Dependent Calcium-Binding Proteins in Mammalian Kidney

Immunocytochemical Demonstration of Two Vitamin D-Dependent Calcium-Binding Proteins in Mammalian Kidney

Calbindin‐D28K and the peptidergic neuroendocrine system in rat gut: an immunohistochemical study

Calcium-Binding Proteins in Serum of Chickens: Vitellogenin and Albumin

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Calbindin‐D_28K and the peptidergic neuroendocrine system in rat gut: an immunohistochemical study