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S H Barondes

Publications and source records attributed to S H Barondes.

At least 19 recordsLinked to original sources
PubMed1992

Sequence and specificity of a soluble lactose-binding lectin from Xenopus laevis skin.

A 16-kDa lactose-binding lectin comprises 5% or more of the soluble protein in Xenopus laevis skin. This lectin is mainly localized in the cytoplasm of granular gland cells. In response to stress, the lectin along with a variety of toxic and antibiotic peptides are released onto the skin surface by holocrine secretion. We have purified the lectin, sequenced tryptic peptides using tandem mass spectrometry and Edman degradation, and isolated full-length cDNA using a deduced oligonucleotide. Comparison of the cDNA and peptide sequences revealed expression of at least two isolectins, which differ in sequence at only two or three amino acids. Comparison of cDNA with complementary message by ribonuclease protection confirmed expression in approximately equal abundance of two nearly identical messages. The major soluble lactose-binding lectin expressed in Xenopus muscle is composed of these same isolectins, but at 100-fold lower levels. Similarities and distinctions in sequence and carbohydrate-binding specificity indicate that this lectin is a novel member of a family of soluble lactose-binding lectins expressed in a wide range of vertebrate tissues.

Amino Acid Sequence↗
PubMed1992

Isolation and expression of a gene encoding L-14-II, a new human soluble lactose-binding lectin.

In the course of screening a human hepatoma cDNA library with antibody raised against a mammalian lectin with subunit molecular weight of about 14,000, we detected a partial cDNA encoding a related but distinct protein that was possibly a homologous lectin (Gitt and Barondes, 1986). We here report the isolation and sequencing of a full-length cDNA for this protein from a HepG2 cDNA library. The cDNA encodes a protein with subunit molecular weight of 14,650. Expression of the coding sequence in Escherichia coli yields a product that binds to a lactose affinity column and is specifically eluted with lactose, confirming that this new protein is a lectin. Like its well studied relative, here called L-14-I, the new lectin, L-14-II, exists as a homodimer in solution. The two related human lectins have 43% amino acid sequence identity. The genomic DNA encoding L-14-II (LGALS2) contains four exons with similar intron placement to L-14-I (LGALS1); but the genomic upstream region, which contains several sequences characteristic of regulatory elements, differs significantly from L-14-I.

Amino Acid Sequence↗
PubMed1992

How genetically heterogeneous are the major psychiatric disorders?

Linking specific chromosomal regions with the abnormal genes responsible for major psychiatric disorders is rendered particularly difficult because of three factors: diagnostic uncertainty; the possibility that some psychiatric disorders are caused by the concerted action of more than one gene; and the possibility that similar disorders may result from alternative genetic abnormalities. The approach proposed here is to concentrate initially on the highly focused problem of resolving the question of genetic heterogeneity of a given disorder. To this end, it is recommended (a) that studies concentrate on pedigrees large enough to contain at least two nuclear families with several affected individuals, and (b) that, within them, work be confined to an intensive examination of such small nuclear families containing an affected parent and at least two affected offspring with a fairly unmistakable phenotype--bipolar disorder, type I. By using molecular and genetic techniques designed to extract maximal information from this relatively small number of affected individuals, it should be possible to determine whether or not bipolar disorder is genetically heterogeneous. This is a limited but very important question, and the technology is presently available to answer it. The answer should, in turn, guide subsequent approaches to identification of the relevant gene or genes.

Bipolar Disorder↗
PubMed1991

Human breast carcinoma cDNA encoding a galactoside-binding lectin homologous to mouse Mac-2 antigen.

A galactoside-binding lectin (Mr 29,000) has previously been identified in rat, mouse and human tissues. It is an abundant cell-surface component of inflammatory macrophages and their major non-integrin laminin-binding protein. It has also been found in the nucleus of other cell types. Here, we report the cloning and sequencing of a cDNA encoding the human galactoside-binding lectin from a breast carcinoma. The clone encodes a protein of 250 amino acids (aa) that is over 80% identical to its mouse and rat counterparts. The aa sequence has an N-terminal and a C-terminal, 'carbohydrate-binding', domain. The N-terminal domain consists of two parts. The first 41 aa are homologous to a transcription factor, i.e., the serum response factor. The adjacent part (aa 42-106) contains an unusual repeating element, that occurs seven times in human protein compared to nine times in rat and mouse. The C-terminal 'carbohydrate-binding' domain (aa 115-250) shows homology to L-14, another galactoside-binding lectin.

Amino Acid Sequence↗
PubMed1991

Genomic sequence and organization of two members of a human lectin gene family.

We have isolated and sequenced the genomic DNA encoding a human dimeric soluble lactose-binding lectin. The gene has four exons, and its upstream region contains sequences that suggest control by glucocorticoids, heat (environmental) shock, metals, and other factors. We have also isolated and sequenced three exons of the gene encoding another human putative lectin, the existence of which was first indicated by isolation of its cDNA. Comparisons suggest a general pattern of genomic organization of members of this lectin gene family.

Amino Acid Sequence↗
PubMed1991

Endogenous muscle lectin inhibits myoblast adhesion to laminin.

L-14, a dimeric lactose-binding lectin with subunits of 14 kD, is expressed in a wide range of vertebrate tissues. Several functions have been postulated for this lectin, but definitive evidence for a specific biological role has been elusive. In muscle, L-14 is secreted during differentiation and accumulates with laminin in basement membrane surrounding each myofiber. Here we present evidence that laminin is a major glycoprotein ligand for L-14 in differentiating mouse C2C12 muscle cells and that binding of secreted L-14 to polylactosamine oligosaccharides of substrate laminin induces loss of cell-substratum adhesion. These results suggest that one function of L-14 is to regulate myoblast detachment from laminin during differentiation and fusion into tubular myofibers.

Animals↗
PubMed1990

Evidence for export of a muscle lectin from cytosol to extracellular matrix and for a novel secretory mechanism.

A soluble lactose-binding lectin with subunit Mr of 14,500 is believed to function by interacting with extracellular glycoconjugates, because it has been detected extracellularly by immunohistochemistry. This localization has been questioned, however, since the lectin lacks a secretion signal sequence, which challenges the contention that it is secreted. We have demonstrated externalization of this lectin from C2 mouse muscle cells by both immunoprecipitation of metabolically labeled protein and immunohistochemical localization. We further show that externalization of the lectin is a developmentally regulated process that accompanies myoblast differentiation and that the lectin codistributes with laminin in myotube extracellular matrix. Immunohistochemical localization during intermediate stages of externalization suggests that the lectin becomes concentrated in evaginations of plasma membrane, which pinch off to form labile lectin-rich extracellular vesicles. This suggests a possible mechanism for lectin export from the cytosol to the extracellular matrix.

Amino Acid Sequence↗
PubMed1990

Selective expression of an endogenous lactose-binding lectin gene in subsets of central and peripheral neurons.

Cellular interactions in a variety of vertebrate non-neural tissues are thought to be mediated by cell surface carbohydrate structures. The detection of cell-specific surface carbohydrates and carbohydrate-binding proteins within the embryonic nervous system has raised the possibility that carbohydrate recognition may also contribute to the interactions of developing neurons. Soluble lactose-binding lectins constitute one class of carbohydrate-binding proteins expressed in the vertebrate nervous system. We describe here the isolation of cDNAs from rat brain libraries encoding one of these lectins, RL-14.5, and demonstrate that this protein is not only homologous to other soluble lectins, but also identical in primary sequence to a lectin present in at least one non-neural tissue. RNA blot analysis and in situ hybridization reveal a restricted pattern of expression of RL-14.5 mRNA within the rat nervous system. High levels of RL-14.5 mRNA are present in primary sensory neurons and motoneurons in the spinal cord and brain stem. Moreover, expression of RL-14.5 mRNA in sensory and motoneurons is detectable soon after neuronal differentiation. These findings, together with previous studies demonstrating the selective expression of oligosaccharide ligands for RL-14.5 on the same neurons, are consistent with the idea that carbohydrate-mediated interactions contribute to the development of this subset of mammalian neurons.

Amino Acid Sequence↗
PubMed1989

Soluble lactose-binding vertebrate lectins: a growing family.

Extracts of rat intestine contain nine soluble lactose-binding lectins with subunit molecular weights ranging from 14,500 to 19,000 that were purified by affinity chromatography and ion-exchange chromatography. Two of them are either identical with or closely related to other known rat lectins. A third appears to be the isolated carbohydrate-binding C-terminal domain of a known lectin but lacks the N-terminal domain presumed to mediate a different function. The others have not been described previously. Among them, the major rat intestinal lectin, RI-H, and a related protein, RI-G, have N-terminal amino acid sequences with similarities to sequences found in other known rat lectins. Therefore, these results introduce new members of a growing family of these structurally homologous soluble lactose-binding proteins.

Amino Acid Sequence↗
PubMed1988

The elastin receptor: a galactoside-binding protein.

The elastin receptor complex contains a component of 67 kilodaltons that binds to a glycoconjugate affinity column containing beta-galactoside residues and is eluted from this column with lactose. This protein component is also released from the surface of cultured chondroblasts by incubation with lactose, and its association with immobilized elastin is inhibited by lactose. Since lactose also blocks elastic fiber formation by cultured chondroblasts, the galactoside-binding property of the elastin receptor is implicated in this process.

Animals↗
PubMed1988

Endogenous lectin secretion into the extracellular matrix of early embryos of Xenopus laevis.

An endogenous galactoside-binding lectin with subunit molecular weight of 43,000-45,000, previously detected in unfertilized eggs of Xenopus laevis, persists at high levels in embryos through gastrulation. During embryonic development the lectin is found in cytoplasmic vesicles, and then is secreted into extracellular matrix which is prominent around the blastopore and on the roof of the blastocoel. The lectin is also found in the extracellular material in the developing neural fold. The presence of lectin at sites of active morphogenetic movements raises the possibility that it participates in the formation of an extracellular matrix that influences these processes.

Animals↗
PubMed1988

Multiple soluble vertebrate galactoside-binding lectins.

All vertebrates synthesize soluble galactoside-binding lectins. Many are expressed at high levels in the embryo and at lower levels in the adult, whereas others show an inverse pattern of expression. Most lectins tend to be concentrated in one or a number of specific cell types. In the past few years, the multiplicity of these lectins has become more apparent. For example, in Xenopus laevis 3 galactoside-binding lectins, 2 with a preference for alpha-galactosides, have been purified and partially characterized. They have subunit molecular weights ranging from 16,000 to 69,000. More detailed studies have been done in mammals. For example, rat lung contains 3 soluble beta-galactoside-binding lectins, RL-14.5, RL-18 and RL-29, with subunit molecular weights, respectively, of 14,500, 18,000 and 29,000. A notable feature of these lectins is that, although they all bind lactose about equally well, their carbohydrate-binding sites are actually quite different, as shown by competitive binding studies with a range of complex mammalian glycoconjugates. Human lung also contains several beta-galactoside-binding lectins, including HL-14, HL-22 and HL-29 with subunit molecular weights, respectively, of 14,000, 22,000 and 29,000. They too show significant differences in their carbohydrate-binding sites when analyzed with naturally occurring mammalian glycoconjugates. Sequencing of purified lectins and cDNA clones indicates that at least 4 distinct genes code for what appears to be a family of HL-14. Heterogeneity is also indicated from isoelectric focusing studies which resolve at least 6 acidic forms of HL-14 and 5 acidic forms of HL-29.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acid Sequence↗
PubMed1987

Multiple soluble beta-galactoside-binding lectins from human lung.

Soluble extracts of human lung contain three major beta-galactoside-binding proteins with apparent subunit molecular weights of 14,000 (HL-14), 22,000 (HL-22), and 29,000 (HL-29). HL-14 and HL-29 were abundant in all the specimens that we tested whereas HL-22 was abundant in some and very scarce in others. HL-14 could be resolved into at least six acidic forms by isoelectric focusing and HL-29 into at least five acidic forms by this procedure. In contrast, HL-22 is a basic protein. Other beta-galactoside-binding proteins with subunit molecular weights ranging from about 16,000 to 27,000 were also detected in lung extracts, but the possibility that they are degradation products cannot be excluded. HL-14 is very similar to a rat lung lectin (RL-14.5) in carbohydrate binding specificity and amino acid composition and reacts strongly with an antiserum raised against the rat lectin. HL-29 is similar to the rat lectin RL-29 in the same respects, but its carbohydrate binding specificity is somewhat different. Of the known rat lectins, HL-22 resembles RL-18 most closely in carbohydrate binding specificity, but it is significantly different in other properties and does not react with an antiserum raised against the rat lectin.

Amino Acids↗