Calbindin in vertebrate classes: Immunohistochemical localization and Western blot analysis

Parmentier, Marc; Ghysens, M.; Rypens, Françoise; Lawson, David; Pasteels, Jean-Lambert; Pochet, Roland

doi:10.1016/0016-6480(87)90125-0

Cited by 91 publications

(48 citation statements)

References 19 publications

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“…Western blots of calbindin labeled major and minor bands of ϳ28 and 30 kDa (Fig. 5), similar to the molecular weights observed previously in rat and human brains (Parmentier et al, 1987).…”

Section: Protein Levels Of Candidate Neuroadaptationssupporting

confidence: 86%

Long-Term Upregulation of Protein Kinase A and Adenylate Cyclase Levels in Human Smokers

Hope¹,

Nagarkar²,

Leonard³

et al. 2007

J. Neurosci.

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Repeated injections of cocaine and morphine in laboratory rats cause a variety of molecular neuroadaptations in the cAMP signaling pathway in nucleus accumbens and ventral tegmental area. Here we report similar neuroadaptations in postmortem tissue from the brains of human smokers and former smokers. Activity levels of two major components of cAMP signaling, cAMP-dependent protein kinase A (PKA) and adenylate cyclase, were abnormally elevated in nucleus accumbens of smokers and in ventral midbrain dopaminergic region of both smokers and former smokers. Protein levels of the catalytic subunit of PKA were correspondingly higher in the ventral midbrain dopaminergic region of both smokers and former smokers. Protein levels of other candidate neuroadaptations, including glutamate receptor subunits, tyrosine hydroxylase, and other protein kinases, were within normal range. These findings extend our understanding of addiction-related neuroadaptations of cAMP signaling to tobacco smoking in human subjects and suggest that smoking-induced brain neuroadaptations can persist for significant periods in former smokers.

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Section: Protein Levels Of Candidate Neuroadaptationssupporting

confidence: 86%

Long-Term Upregulation of Protein Kinase A and Adenylate Cyclase Levels in Human Smokers

Hope¹,

Nagarkar²,

Leonard³

et al. 2007

J. Neurosci.

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“…In lower vertebrates and specially in fish their distribution has been reported to be restricted to neural circuits [ 11,20]. However, the present investigation demonstrates for the first time the presence of calbindin D28K in the gill epithelium of fish.…”

Section: Discussionmentioning

confidence: 44%

“…A phylogenetic survey of calbindin distribution shows that this protein has an old history and is highly conserved in the vertebrates including fish. In the latter calbindin has been described in the brain and not in kidney or gut [11].…”

Section: Introductionmentioning

confidence: 99%

Localization of calbindin D28K-like immunoreactivity in fish gill: a light microscopic and immunoelectron histochemical study

Zaccone

Bonga

Flik

et al. 1992

Regulatory Peptides

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SummaryThe presence of calbindin D28K in fish (Heteropneustes fossilis) gill was studied by use of specific antibodies raised against chick duodenal 28 kD a calbindin in immunoperoxidase and electron-microscopic labelling experiments. Immunoreactivity for calbindin D28K, which has been observed in the intestine of a number of avian and mammalian species, is reported for the first time in the gill. It was primarily located in neuroendocrine (NE) cells. Some immunoreactivity was also located in the glycocalyx of the non-endocrine cells, i.e., the pavement cells, which have ultrastructural characteristics quite different from those of endocrine cells.The calbindin-immunopositive NE cells were ascertained in both gill filamental and lamellar epithelium. All the NE cells contained secretory granules as the most distinc tive feature of these cells. Ultrastructurally, two types of NE cells were distinguished according to the morphology of their secretory granules.The calbindin immunoreactivity in the NE cells was stimulated when the calcium concentration of the ambient water was rcduccd. The present findings suggest that NE

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“…Both proteins play equivalent roles in the intestinal control of calcium absorption, though their evolutionary rates are greatly dissimilar. We showed previously that, from an evolutionary point of view, calbindin was primarily a neuronal protein [12]. It can be postulated, therefore, that the functions in neurons and intestinal absorptive cells could be different.…”

Section: Discussionmentioning

confidence: 99%

“…In a previous work we described two different proteins presenting calbindin immunoreactivity in the central nervous system, of molecular mass 27-kDa and 29-kDa respectively [l I]. More recently we showed that both molecular species were present in the brain of all vertebrates with the exception of the fish [12]. It is still unclear whether these two proteins are the result of alternative messenger RNA splicing or are encoded by distinct genes.…”

mentioning

confidence: 99%

Human 27‐kDa calbindin complementary DNA sequence

Parmentier

Lawson

Vassart

1987

European Journal of Biochemistry

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Human 27‐kDa calbindin cDNA clones were selected by antibody screening from λgt11 brain libraries. The sequence revealed an open reading frame coding for a protein of 261 amino acids, containing four active calcium‐binding domains, and two modified domains that had presumably lost their calcium‐binding capability. Comparison with chick and bovine calbindins showed that the protein was highly conserved in evolution (evolutionary rate: 0.3 × 10−9 amino acid−1 year−1) and that active and inactive domains were equally conserved. From the data we postulate that calbindin has an important physiological function involving protein–protein interactions. Comparison of calcium‐binding domains from various proteins suggested that all members of the troponin C superfamily derive from a common two‐domained ancestor, but that duplications leading to calbindin and to the four‐domained calcium‐binding proteins took place independently on different branches of the evolutionary tree. Preliminary data showed that another calcium‐binding protein, homologous to calbindin, is present in the brain and encoded by a different gene.

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Calbindin in vertebrate classes: Immunohistochemical localization and Western blot analysis

Cited by 91 publications

References 19 publications

Long-Term Upregulation of Protein Kinase A and Adenylate Cyclase Levels in Human Smokers

Long-Term Upregulation of Protein Kinase A and Adenylate Cyclase Levels in Human Smokers

Localization of calbindin D28K-like immunoreactivity in fish gill: a light microscopic and immunoelectron histochemical study

Human 27‐kDa calbindin complementary DNA sequence

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