Chick endogenous lectin enhances chondrogenesis of cultured chick limb bud cells

Matsutani, Etsuya; Yamagata, Toshio

doi:10.1016/0012-1606(82)90199-3

Cited by 26 publications

(10 citation statements)

References 22 publications

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“…The CG-1A activity reported appears to underlie the observations in a study from nearly three decades ago [56] describing enhancement in the number of chicken limb precartilage condensations in vitro by a lectin from adult liver. Our initial studies of CG-1A expression, which suggested that this galectin was expressed earlier in vitro than fibronectin (up to now the best candidate for an ECM mediator of condensation; [11,12,47], and indeed earlier than ligands for PNA, these epitopes being among the earliest so far known molecular condensation markers [35,36], warranted pursuing detailed expression and functional studies with this and the other four CGs.…”

Section: Discussionsupporting

confidence: 58%

A regulatory network of two galectins mediates the earliest steps of avian limb skeletal morphogenesis

et al. 2011

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BackgroundThe skeletal elements of vertebrate embryonic limbs are prefigured by rod- and spot-like condensations of precartilage mesenchymal cells. The formation of these condensations depends on cell-matrix and cell-cell interactions, but how they are initiated and patterned is as yet unresolved.ResultsHere we provide evidence that galectins, β-galactoside-binding lectins with β-sandwich folding, play fundamental roles in these processes. We show that among the five chicken galectin (CG) genes, two, CG-1A, and CG-8, are markedly elevated in expression at prospective sites of condensation in vitro and in vivo, with their protein products appearing earlier in development than any previously described marker. The two molecules enhance one another's gene expression but have opposite effects on condensation formation and cartilage development in vivo and in vitro: CG-1A, a non-covalent homodimer, promotes this process, while the tandem-repeat-type CG-8 antagonizes it. Correspondingly, knockdown of CG-1A inhibits the formation of skeletal elements while knockdown of CG-8 enhances it. The apparent paradox of mutual activation at the gene expression level coupled with antagonistic roles in skeletogenesis is resolved by analysis of the direct effect of the proteins on precartilage cells. Specifically, CG-1A causes their aggregation, whereas CG-8, which has no adhesive function of its own, blocks this effect. The developmental appearance and regulation of the unknown cell surface moieties ("ligands") to which CG-1A and CG-8 bind were indicative of specific cognate- and cross-regulatory interactions.ConclusionOur findings indicate that CG-1A and CG-8 constitute a multiscale network that is a major mediator, earlier-acting than any previously described, of the formation and patterning of precartilage mesenchymal condensations in the developing limb. This network functions autonomously of limb bud signaling centers or other limb bud positional cues.

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Section: Discussionsupporting

confidence: 58%

A regulatory network of two galectins mediates the earliest steps of avian limb skeletal morphogenesis

et al. 2011

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“…The strict regulation of galectin-3 expression in developing bones strongly suggests a role in these processes. We note that another member of the same gene family may also be involved in chondrogenesis since previous reports have shown that a chick 16 kD galactoside specific lectin is able to initiate the formation of cartilaginous cells from limb bud mesenchyme cells (Matsutani and Yamagata, 1982).…”

Section: Expression In the Skeletal Systemmentioning

confidence: 78%

Galectin‐3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo

Fowlis

Colnot

Ripoche

et al. 1995

Developmental Dynamics

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The galectins are a family of low molecular weight, calcium-independent mammalian carbohydrate binding proteins that exhibit specificity for beta-galactoside derivatives. We have examined the expression pattern of galectin-3 in the developing mouse embryo by in situ hybridisation and immunohistochemistry. In the embryo proper, galectin-3 message and protein are first detected in notochord, starting from 8.5 days post coitum (dpc), and persist until this structure disappears. Galectin-3 is later found in cartilage primordia and in developing skin from 13.5 dpc. This very restricted and dynamic pattern suggests that galectin-3 may participate in the establishment and/or maintenance of notochord as well as the formation of cartilage and differentiation of skin. Finally, we find that galectin-3, which is identical to the macrophage marker Mac-2, is also expressed in embryonic macrophages. 0 1995 Wiley-Liss, Inc.

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“…The two lectins are also differentially expressed during differentiation of the brain, liver, heart, skeletal muscle, stomach and skin (Kitamura 1980;Kobiler and Barondes 1977;Kobiler et al 1978;Oda and Kasai 1983;Sakakura et al 1990). These proteins are mitogenic (Lipsick et al 1980;Pitts and Yang 1981), and the 16 kD lectin has been reported to enhance chondrogenesis in cultures of dissociated limb bud cells (Matsutani and Yamagata 1982). In the developing embryonic skin, at the initial stages of feather differentiation, a 16.5 kD lectin has been localized in the epidermis and dermis; in the latter, the lectin exhibits a localization similar to that of fibronectin (Kitamura 1981).…”

Section: Embryogenesismentioning

confidence: 99%

On the possible role of endogenous lectins in early animal development

Zalik

1991

Anat Embryol

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In this review I have tried to summarize the information available on the lectins of developing embryos. The emerging evidence indicates that during fertilization carbohydrate-binding proteins play a role in sperm adhesion and in the reorganization of the extracellular matrix of the fertilized egg. Results also indicate that in adult tissues lectins participate in cell recognition and adhesion, and that several galactose-binding lectins function as receptors for laminin and, in principle could also interact with polylactosamine groups of other extracellular matrix glycoproteins. Since in developing embryos lectins are located at the cell surface, and colocalize with extracellular matrix glycoproteins, they could play a role in transitory adhesive interactions and in the segregation of organ primordia. On the basis of experiments in cultured cell lines, it has been suggested that lectins are involved in lysosomal and nuclear glycoprotein transport. These carbohydrate-binding proteins could also regulate development by modulating these processes in the embryo. Since galactose-binding lectins are mitogenic, and are present in high concentration in the chick yolk sac, these proteins could be released into the embryonic circulation, bind to cells expressing appropriate receptors, and act as growth regulators, by modulating cell division of specific cell lineages.

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Chick endogenous lectin enhances chondrogenesis of cultured chick limb bud cells

Cited by 26 publications

References 22 publications

A regulatory network of two galectins mediates the earliest steps of avian limb skeletal morphogenesis

A regulatory network of two galectins mediates the earliest steps of avian limb skeletal morphogenesis

Galectin‐3 is expressed in the notochord, developing bones, and skin of the postimplantation mouse embryo

On the possible role of endogenous lectins in early animal development

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