Genomic structure of the human caldesmon gene.

Hayashi, Ken’ichiro; Yano, Hajime; Hashida, Takashi; Takeuchi, Rie; Takeda, Osamu; Asada, Kiyozo; Takáhashi, Eiichi; Kato, Ikuo; Sobue, Kenji

doi:10.1073/pnas.89.24.12122

Cited by 89 publications

(97 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The resulting cDNA was amplified by PCR using CALD1 specific primer sets spanning the splice sites of this gene toward all of the four splicing variants of l-CaD as described elsewhere. 7 A primer set for the CALD1, designed to amplify all of the splicing variants, 25 was used for initial examining the microdissected samples (the product size for l-CaD isoforms is 744 bp). Glyceraldehyde 3-phosphate dehydrogenase (GAPD) fragment 26 was prepared by PCR as an internal control.…”

Section: Cald1 Transcript Analysismentioning

confidence: 99%

“…4 -6 The caldesmon gene (CALD1) is a single gene with transcriptional variance characterized by the recombination of different alternative splicing modes regulated by specific promoter activities. 7 The human CALD1 shares common structural and expressional properties through mammals. 8,9 The gene is located on chromosome 7q33-34, consists of at least 15 exons and gives rise to two major classes of protein isoforms, ie, high molecular weight caldesmon (120 to 150 kd, h-CaD) and low molecular weight caldesmon (70 to 80 kd, l-CaD).…”

mentioning

confidence: 99%

“…8,9 The gene is located on chromosome 7q33-34, consists of at least 15 exons and gives rise to two major classes of protein isoforms, ie, high molecular weight caldesmon (120 to 150 kd, h-CaD) and low molecular weight caldesmon (70 to 80 kd, l-CaD). 7,10 The conserved regions of all isoforms encoded by exon 2, 3a, and 5 to 15 contain caldesmons' capacity to bind to actin, tropomyosin, Ca (2ϩ)-calmodulin, myosin, and phospholipids. 11 The exons 1, 3b, and 4 are alternatively spliced.…”

mentioning

confidence: 99%

“…l-CaD consists of at least four splicing variants (WI-38 l-CaDs I and II, Hela l-CaDs I and II) which are expressed via differential inclusion of the variable alternative spliced exons 1, 1Ј and 4 of the gene. 7 The exons 1 and 1Ј encode the short amino terminus specific for Hela l-CaDs and WI-38 l-CaDs or h-CaD, respectively. 7 The l-CaD isoforms are ubiquitously distributed in various cells and dedifferentiated SMCs.…”

mentioning

confidence: 99%

“…7 The exons 1 and 1Ј encode the short amino terminus specific for Hela l-CaDs and WI-38 l-CaDs or h-CaD, respectively. 7 The l-CaD isoforms are ubiquitously distributed in various cells and dedifferentiated SMCs. They play roles in the regulation of cell contractility, adhesion-dependent signaling, and cytoskeletal organization, influencing granule movement, hormone secretion, and reorganization of microfilaments during mitosis via mitosis-specific phosphorylation by cdc2 protein kinase.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Differential Expression of Splicing Variants of the Human Caldesmon Gene (CALD1) in Glioma Neovascularization versus Normal Brain Microvasculature

Zheng

Sieuwerts

Luider

et al. 2004

The American Journal of Pathology

View full text Add to dashboard Cite

Caldesmon is a cytoskeleton-associated protein whichhas not yet been related to neoplastic angiogenesis. In this study we investigated the expression of the caldesmon gene (CALD1) splicing variants and the protein expression level in glioma microvessels versus normal brain microvasculature. To exclude sources of splice variant expression from non-vascular components all possible cellular components present in control and glioma samples were prescreened by laser-capture microdissection followed by RT-PCR before the cohort study. We discovered differential expression of the splicing variants of CALD1 in the tumor microvessels in contrast to normal brain microvasculature. Missplicing of exons 1, 1 ؉ 4, and 1 ؉ 4 of the gene is exclusively found in glioma microvessels. To exclude the possibility that this missplicing results from splice-site mutations, Genome-wide analyses have revealed that 40 to 60% of human genes undergo alternative splicing. 1 Alternative splicing, therefore, seems to contribute considerably to enable the highly complex and diverse functions encoded by the human genome. Alternative splicing permits vertebrate pre-mRNA to be processed into multiple mRNAs differing in their precise combination of exon sequences, resulting in the encoding of different protein isoforms. 2 Multiple modes of alternative splicing exist, such as alternative 5Ј or 3Јsplice-site usage, differential inclusion or skipping of particular exons, mutually exclusion of exons, and more. 3 Importantly, alternative splicing is often tightly regulated in a cell type-or developmental stage-specific mode. 3 The essential nature of this process is underscored by the fact that misregulation (missplicing events) is often related to human disease. 4 -6

show abstract

Section: Cald1 Transcript Analysismentioning

confidence: 99%

mentioning

confidence: 99%