Genomic Cloning of the Human Histo-Blood Group ABO Locus

Bennett, Eric; Steffensen, Rudi; Clausen, Henrik; Weghuis, D.E.M. Olde; Kessel, A.H.M. Geurts van

doi:10.1006/bbrc.1995.1044

Cited by 116 publications

(70 citation statements)

References 3 publications

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“…36 The ABO gene, located on the telomeric end of the long arm of human chromosome 9 (9q34), encodes for enzymes that produce the major antigens in the ABO blood group system (fig 1). 37 The fact that some studies found an association between the ABO blood groups, a biochemical marker for variants of the ABO gene, and Achilles tendon pathology justifies investigating this region of chromosome 9 for potential candidate genes for Achilles tendon injuries. 19 31 38 It should be noted that the lack of association (ie, a negative result) of the ABO blood group with Achilles tendon injuries in some studies does not imply that one can exclude the existence of a causal variant either at the ABO locus or in close proximity (adjacent gene/s).…”

Section: Achilles Tendon Injuriesmentioning

confidence: 99%

Tendon and ligament injuries: the genetic component

September

Schwellnus²,

Collins³

2007

Br J Sports Med

133

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Tendons and ligaments within the upper and lower limbs are some of the more common sites of musculoskeletal injuries during physical activity. Several extrinsic and intrinsic factors have been shown to be associated with these injuries. More recently, studies have suggested that there is also, at least in part, a genetic component to the Achilles tendon, rotator cuff and anterior cruciate ligament injuries. However, specific genes have not been suggested to be associated with rotator cuff or anterior cruciate ligament injuries. Sequence variants of the tenascin C (TNC) gene, on the other hand, have been shown to be associated with Achilles tendinopathies and Achilles tendon ruptures, whereas a variant of the collagen V α 1 (COL5A1) gene has also been shown to be associated with Achilles tendinopathies. Both genes encode for important structural components of tendons and ligaments. TheCOL5A1gene encodes for a component of type V collagen, which has an important role in regulating collagen fibre assembly and fibre diameters. TheTNCgene, on the other hand, encodes for TNC, which regulates the tissue’s response to mechanical load. To date, only variants in two genes have been shown to be associated with Achilles tendon injuries. In addition, although specific genes have not been identified, investigators have suggested that there is also a genetic component to both rotator cuff and anterior cruciate ligament injuries. In future, specific genotypes associated with increased risk of injury to specific tendons and ligaments can prevent these injuries by identifying individuals at higher risk.

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Section: Achilles Tendon Injuriesmentioning

confidence: 99%

Tendon and ligament injuries: the genetic component

September

Schwellnus²,

Collins³

2007

Br J Sports Med

133

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“…Expression of the pAcGP67-GalNAc-T2-sol construct resulted in an almost 50-fold increase in GalNAc-transferase activity using the Muc2 substrate-peptide in the culture medium of infected cells compared with uninfected controls as well as cells infected with the blood group A glycosyltransferase (Bennett et al, 1995) (Table III). Similarly, a 50-fold increase was observed using the hCG peptide.…”

Section: Expression Of Galnac-transferase (Galnac-t2)mentioning

confidence: 99%

Purification and cDNA Cloning of a Human UDP-N-acetyl-α- D-galactosamine:polypeptide N-Acetylgalactosaminyltransferase

White

Bennett

Takio

et al. 1995

Journal of Biological Chemistry

195

155

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A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) from human placenta was purified to apparent homogeneity using a synthetic acceptor peptide as affinity ligand. The purified GalNAc-transferase migrated as a single band with an approximate molecular weight of 52,000 by reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Based on a partial amino acid sequence, the cDNA encoding the transferase was cloned and sequenced from a cDNA library of a human cancer cell line. The cDNA sequence has a 571-amino acid coding region indicating a protein of 64.7 kDa with a type II domain structure. The deduced protein sequence showed significant similarity to a recently cloned bovine polypeptide GalNAc-transferase (Homa, F. L., Hollanders, T., Lehman, D. J., Thomsen, D. R., and Elhammer, Å. P. (1993) J. Biol. Chem. 268, 12609 -12616). A polymerase chain reaction construct was expressed in insect cells using a baculovirus vector. Northern analysis of eight human tissues differed clearly from that of the bovine GalNAc-transferase. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level was found. The data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members.

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“…6) was determined by comparing the A(1) cDNA sequence with A(1) containing rat genomic DNA (GenBank TM accession numbers AF296761, AF469947, and AF469948). All exon-intron boundaries conformed to the GT-AG consensus rule (not shown), and their number and localization were similar to the human blood group A glycosyltransferase gene (27,28).…”

Section: Genbankmentioning

confidence: 73%

“…The reactions were analyzed on an ALF Express using the ReproGel TM Long Read (Amersham Biosciences). cDNA Cloning and Construction of Expression Plasmids-The 7.5-kb rat genomic DNA sequence was compared with the seven exons of the human blood group A glycosyltransferase (27,28) and was found to contain regions similar to human exons 3-7. From this, a partial cDNA sequence of the rat transferase was proposed, containing the stop codon in exon 7.…”

Section: Infection Of Rats By the Nematode N Brasiliensis And Isolatmentioning

confidence: 99%

Blood Group A Glycosyltransferase Occurring as Alleles with High Sequence Difference Is Transiently Induced during aNippostrongylus brasiliensis Parasite Infection

Olson¹,

Johansson²,

Klinga-Levan³

et al. 2002

Journal of Biological Chemistry

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Neutral mucin oligosaccharides from the small intestine of control rats and rats infected with the parasite Nippostrongylus brasiliensis were released and analyzed by gas chromatography-mass spectrometry. Infected animals expressed seven blood group A-like structures that were all absent in the control animals. The blood group A nature of these epitopes was confirmed by blood group A reactivity of the prepared mucins, of which Muc2 was one. Transferase assays and Northern blotting on small intestines from infected animals showed that an ␣-N-acetylgalactosaminyltransferase similar to the human blood group A glycosyltransferase had been induced. The expression was a transient event, with a maximum at day 6 of the 13-daylong infection. The rat blood group A glycosyltransferase was cloned, revealing two forms with an amino acid similarity of 95%. Both types had blood group A transferase activity and were probably allelic because none of 12 analyzed inbred strains carried both types. The second type was found in outbred rats and in one inbred strain. First generation offspring of inbred rats of each type were heterozygous, further supporting the allelic hypothesis. The transient induction and the large allelic variation could suggest that glycosyltransferases are part of a dynamic system altering mucins and other glycoconjugates as a protecting mechanism against microbial challenges.The gastrointestinal tract is covered by a mucus layer, effectively protecting the epithelial cells from the hostile milieu including microorganisms and at the same time allowing digested nutrients and other smaller molecules to traverse. Microorganisms bind to intestinal mucus and epithelial cells; some of this binding is with high specificity to glycan epitopes (1). To maintain the protective layer despite continuous damaging processes, especially by these intestinal microorganisms, a system with a continuous mucus renewal is demanded. In the intestine, a majority of the mucus is produced by the goblet cells interspersed between the enterocytes. The matrix in the mucus is made up of gel-forming mucins. These are highly glycosylated proteins, where up to 80% of the mass is from O-linked oligosaccharides. Cloning and sequencing of mucin genes have revealed that the sites for glycosylation are located in domains of long stretches of protease-resistant sequences rich in the amino acids serine and threonine together with proline. Because these domains are typical for mucins, but also found in other proteins, they have been named mucin domains. Up until now, 13 human mucin genes have been identified and fully or partly sequenced (2-4), in addition to mucins identified from other species. The major intestinal mucin in rat is the Muc2 mucin, and the two mucin domains of this mucin have previously been isolated as two highly glycosylated peptides of 650 and 335 kDa, respectively (5, 6). The rat Muc2, as well as its human homologue MUC2, belongs to a class of gel forming mucins, gaining their viscous properties by oligomerization into large mucin...

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Genomic Cloning of the Human Histo-Blood Group ABO Locus

Cited by 116 publications

References 3 publications

Tendon and ligament injuries: the genetic component

Tendon and ligament injuries: the genetic component

Purification and cDNA Cloning of a Human UDP-N-acetyl-α- D-galactosamine:polypeptide N-Acetylgalactosaminyltransferase

Blood Group A Glycosyltransferase Occurring as Alleles with High Sequence Difference Is Transiently Induced during aNippostrongylus brasiliensis Parasite Infection

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