The carbohydrate units of human plasma α1-Acid glycoprotein

Schmid, Karl; Nimberg, Richard B.; Kimura, Atsushi; Yamaguchi, Hisateru; Binette, J. P.

doi:10.1016/0005-2795(77)90080-0

Cited by 151 publications

(89 citation statements)

References 19 publications

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“…Because neither vitronectin nor ␣ 1 -acid glycoprotein bound to preformed complexes of PAI-1, namely, to PAI-1-␣ 1 -acid glycoprotein or PAI-1-vitronectin, respectively, it may be suggested that binding sites for both proteins may be the same or are located in close proximity on the PAI-1 molecule. On the other hand, human ␣ 1 -acid glycoprotein consists of ϳ45% carbohydrates attached in the form of five complex-type N-linked glycans (49,50) that show tetra-antennary as well as di-and tri-antennary structure. The terminating sugars on the glycan chains are responsible for a great deal of the diversity found on glycans, and neuraminic acid is one of the common sugars among them, giving rise to a very low pI.…”

Section: Resultsmentioning

confidence: 99%

Acute Phase Protein α1-Acid Glycoprotein Interacts with Plasminogen Activator Inhibitor Type 1 and Stabilizes Its Inhibitory Activity

Boncela¹,

Papiewska²,

Fijałkowska³

et al. 2001

Journal of Biological Chemistry

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␣ 1 -Acid glycoprotein, one of the major acute phase proteins, was found to interact with plasminogen activator inhibitor type 1 (PAI-1) and to stabilize its inhibitory activity toward plasminogen activators. This conclusion is based on the following observations: (a) ␣ 1 -acid glycoprotein was identified to bind PAI-1 by a yeast two-hybrid system. Three of 10 positive clones identified by this method to interact with PAI-1 contained almost the entire sequence of ␣ 1 -acid glycoprotein; (b) this protein formed complexes with PAI-1 that could be immunoprecipitated from both the incubation mixtures and blood plasma by specific antibodies to either PAI-1 or ␣ 1 -acid glycoprotein. Such complexes could be also detected by a solid phase binding assay; and (c) the real-time bimolecular interactions monitored by surface plasmon resonance indicated that the complex of ␣ 1 -acid glycoprotein with PAI-1 is less stable than that formed by vitronectin with PAI-1, but in both cases, the apparent K D values were in the range of strong interactions (4.51 ؉ 1.33 and 0.58 ؉ 0.07 nM, respectively). The on rate for binding of PAI-1 to ␣ 1 -glycoprotein or vitronectin differed by 2-fold, indicating much faster complex formation by vitronectin than by ␣ 1 -acid glycoprotein. On the other hand, dissociation of PAI-1 bound to vitronectin was much slower than that from the ␣ 1 -acid glycoprotein, as indicated by 4-fold lower k off values. Furthermore, the PAI-1 activity toward urokinase-type plasminogen activator and tissue-type plasminogen activator was significantly prolonged in the presence of ␣ 1 -acid glycoprotein. These observations suggest that the complex of PAI-1 with ␣ 1 -acid glycoprotein can play a role as an alternative reservoir of the physiologically active form of the inhibitor, particularly during inflammation or other acute phase reactions.

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Section: Resultsmentioning

confidence: 99%

Acute Phase Protein α1-Acid Glycoprotein Interacts with Plasminogen Activator Inhibitor Type 1 and Stabilizes Its Inhibitory Activity

Boncela¹,

Papiewska²,

Fijałkowska³

et al. 2001

Journal of Biological Chemistry

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“…Extensive studies have been performed on the glycans present on unfractionated AGP obtained from normal human plasma [2,. It has been reported that tri-and tetraantennary glycans were present in about equal amounts and that about 10% of the glycans were of the diantennary type [8].…”

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confidence: 99%

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Bierhuizen

Wit

Govers

et al. 1988

European Journal of Biochemistry

115

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Human al-acid glycoprotein (AGP) was separated into a non-bound (AGP-A; 46%), a retarded (AGP-B; 39%) and a bound fraction (AGP-C; 150/,) using concanavalin A (ConA) -Sepharose chromatography. The apparent molecular masses, as determined by SDS-PAGE, of the three fractions were 43.5, 42.3 and 41.2 kDa, respectively.The occurrence of N-linked di-, tri-and tetraantennary glycans on these three molecular forms (AGP-A, -B, and -C) was studied by sequential lectin-affinity chromatography of the 14C-labelled glycopeptides. These were obtained by extensive pronase treatment followed by N-[14C]acetylation of the peptide moieties.The glycopeptides of AGP-A did not bind to ConA-Sepharose whereas for AGP-B and AGP-C 18% and 44%, respectively, of the glycopeptides were bound as diantennary structures. Glycopeptide fractions of all three forms of AGP which were not bound to ConA-Sepharose were shown to contain equal amounts of both tri-and tetraantennary glycans by chromatography with Phaseolus vulgaris leukoagglutinating lectin (L-PHA).With the assumption that each molecule contains five glycosylation sites, it could be shown that AGP-A contains no diantennary structures whereas AGP-B and AGP-C contain one and two diantennary structures, respectively. In addition each of the molecular forms contains equal amounts of tri-and tetraantennary structures on the remaining glycosylation sites. The results of this study, therefore, exclude a uniformity of glycan chains in the three molecular forms of AGP.The degree of sialylation of each of the molecular forms was investigated by chromatography on L-PHAagarose and Ricinus communis agglutinin-I -agarose both before and after desialylation of the glycopeptides. It was shown that about 90% of the biantennary glycans of both AGP-B and AGP-C were disialylated while the remainder were monosialylated. The degree of sialylation of the tri-and tetraantennary glycans was identical for the three molecular forms. In each case, one or more terminal galactose residues occurred on at least 20% of the tri-and 65% of the tetraantennary chains.It is suggested that the decrease in the exposure of galactose residues from AGP-A to AGP-C is related to the concomittant decrease in branching of the glycans of the three molecular forms. The relevance of these findings to studies on the function of AGP during inflammatory and liver diseases is discussed. Abbreviations. AGP, ccl-acid glycoprotein; ConA, concanavalin A; L-PHA, Phaseolus vulgaris leukoagglutinating lectin; RCAI, Ricinus communis agglutinin I; CO, LO, RO, non-retarded or nonbound, and Cn, Ln, Rn (n = 1-4) retarded or bound glycopeptide fractions on ConA-Sepharose, L-PHA-agarose and RCA,-agarose, respectively. The fraction names are sometimes used sequentially, e.g. COLlR3, which indicates the fraction of glycopeptides that was not bound on ConA-Sepharose but retarded sequentially on position L1 of L-PHA-agarose and bound on position R3 of RCAI-agarose. Use of the prefix 'a' denotes that the fraction is desialylated by mild acid hydrolysis. fini...

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“…Orosomucoid was prepared from outdated human plasma [19]. p-D-Galactosidase and N-acetyl-p-D-glucosaminidase were prepared from jack bean meal [20].…”

Section: Methodsmentioning

confidence: 99%

Characterization of the high‐affinity oligosaccharide‐binding site of the 205‐kDa porcine large granular lymphocyte lectin, a member of the leukocyte common antigen family

Bezouška

Krajhanzl

Pospísil

et al. 1993

European Journal of Biochemistry

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Membrane lectins of mammalian large granular lymphocytes are thought to be important receptors in their non-major-histocompatibility complex-restricted activation. A triantennary desialylated oligosaccharide has been reported as the most effective triggering structure [Pospilil M., Kubrycht J., Bezoulka K., Tiborsky O., Novhk M. & Kocourek J. (1986) Zmmunol. Lett. 12, 83-90] while its cell surface receptor has recently been identified in pig natural killer cells as a 205-kDa membrane lectin resembling the proteins of the leukocyte common antigen family (LCA). In this study we have prepared 4-azidophenyl (photoactivatable) and 4-hydroxyphenyl (radio-iodinatable) derivatives of triantennary oligosaccharides by a new procedure which allows the natural conformation of the N-glycosidic linkage between the oligosaccharide and the respective labeling group to be retained. We used these high-affinity ligands to investigate the oligosaccharide-combining site of the 205-kDa lectin. Photoaffinity labeling of the whole cells and solubilized proteins confirmed that a 205-kDa polypeptide constitutes the major cell-surface calcium-independent receptor for triantennary oligosaccharides in pig lymphocytes. Isolation and manual sequencing of two ligand-labeled and eleven other peptides proved that the 205-kDa lectin represents a member of the LCA family expressing exons 4 and 6 during alternative splicing and that the high-affinity binding site is localized in the N-terminal 70-kDa extracellular domain. Binding studies with radiolabeled oligosaccharides and the above carbohydrate-recognition domain subjected to various chemical and enzymatic treatments indicated that the binding of oligosaccharides might be significantly modulated by sialylated 0-glycosidically linked lineage-specific carbohydrate epitopes localized within this domain. Affinity chromatography of LCA isolated by conventional methods on immobilized oligosaccharides revealed that only a fraction of these cell-surface glycoproteins expressed high-affinity binding sites for the oligosaccharide ligands. Thus, N-linked oligosaccharide moieties of cell-surface glycoproteins seem to represent possible ligands of LCA that may be important in intercellular adhesion and oligosaccharide-mediated activation of lymphocytes.

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The carbohydrate units of human plasma α1-Acid glycoprotein

Cited by 151 publications

References 19 publications

Acute Phase Protein α1-Acid Glycoprotein Interacts with Plasminogen Activator Inhibitor Type 1 and Stabilizes Its Inhibitory Activity

Acute Phase Protein α1-Acid Glycoprotein Interacts with Plasminogen Activator Inhibitor Type 1 and Stabilizes Its Inhibitory Activity

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Characterization of the high‐affinity oligosaccharide‐binding site of the 205‐kDa porcine large granular lymphocyte lectin, a member of the leukocyte common antigen family

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The carbohydrate units of human plasma α1-Acid glycoprotein

Cited by 151 publications

References 19 publications

Acute Phase Protein α1-Acid Glycoprotein Interacts with Plasminogen Activator Inhibitor Type 1 and Stabilizes Its Inhibitory Activity

Acute Phase Protein α1-Acid Glycoprotein Interacts with Plasminogen Activator Inhibitor Type 1 and Stabilizes Its Inhibitory Activity

Glycosylation of three molecular forms of human α1‐acid glycoprotein having different interactions with concanavalin A

Characterization of the high‐affinity oligosaccharide‐binding site of the 205‐kDa porcine large granular lymphocyte lectin, a member of the leukocyte common antigen family

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Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A