High level of α<sub>1</sub>‐acid glycoprotein in human seminal plasma is associated with high branching and expression of Lewis<sup>a</sup> groups on its glycans: Supporting evidence for a prostatic origin

Poland, Dennis C W; Kratz, Ewa Maria; Vermeiden, Jan P.W.; Groot, Steffen M. De; Bruyneel, Ben; Vries, Theodora de; Dijk, W. van

doi:10.1002/pros.10085

Cited by 22 publications

(21 citation statements)

References 33 publications

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“…The 8.1 galactose, 6.6 fucose, and 10.1 N-acetylglucosamine residues per glycan of PMN AGP were in support to the presence of several lactosamine units (Gal-GlcNAc sequences) per external branch of each glycan, of which the majority is fucosylated. The monosaccharide composition of plasma AGP reflected the well-documented presence of tri-and tetra-antennary N-linked glycans, which do not express considerable amounts of polylactosamine units (i.e., Gal-GlcNAc extensions) [10,11,25]. The sialic acid content of 2.1 residues per glycan was lower than that of plasma AGP (Table 1).…”

Section: Characteristics Of Pmn Agpmentioning

confidence: 92%

“…1a). Treatment for up to 5 min resulted in a timedependent appearance and vanishing of four lower molecular weight bands and the appearance of a 23-kD band, representing the AGP aglycon, being indicative for the presence of five N-linked, complex-type glycans in both AGP preparations [10,25]. Of the two AGP preparations, only PMN AGP stained positively with the monoclonal 6H3 directed against di-or trimeric Lewis X groups (Fig.…”

Section: Characteristics Of Pmn Agpmentioning

confidence: 93%

“…Immortalized human hepatocytes (IHH) were a kind gift of Dr. Han Moshage (University of Groningen, the Netherlands) [24]. Other materials were obtained from commercial sources as described previously [12,25].…”

Section: Methodsmentioning

confidence: 99%

“…Extracts of 3.6 ϫ 10 6 isolated human cardiomyocytes were obtained in the same way. AGP was isolated from the various sources by affinity chromatography on a 1-ml mAb-anti-AGP HiTrap column [25]. AGP concentrations were determined by single radial immunodiffusion according to Mancini et al [35], using polyclonal rabbit anti-human AGP IgG for detection.…”

Section: Cryoimmunogold Electron Microscopymentioning

confidence: 99%

“…Aliqots (50 ng) of AGP were treated and subjected to SDS-PAGE gels with subsequent blotting as described above. Monosaccharide analysis of acid hydrolysates of PNGase F-released glycans was performed by high pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD) [25].…”

Section: N-glycosidase F (Pngase F) Treatment and Monosaccharide Analmentioning

confidence: 99%

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Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Poland¹,

Vallejo²,

Niessen

et al. 2005

Journal of Leukocyte Biology

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␣ 1 -Acid glycoprotein (AGP) is a major acute-phase protein present in human plasma as well as in polymorphonuclear leukocytes (PMN). In this report, we show that PMN synthesize a specific glycoform of AGP, which is stored in the specific and azurophilic granules. Activation of PMN results in the rapid release of soluble AGP. PMN AGP exhibits a substantially higher apparent molecular weight than plasma AGP (50 -60 kD vs. 40 -43 kD), owing to the presence of strongly fucosylated and sialylated polylactosamine units on its five Nlinked glycans. PMN AGP is also released in vivo from activated PMN, as appeared from studies using well-characterized myocard slices of patients that had died within 2 weeks after an acute myocardial infarction. AGP was found deposited transiently on damaged cardiomyocytes in areas with infiltrating PMN only. It is interesting that this was inversely related to the deposition of activated complement C3. Strongly fucosylated and sialylated AGP glycoforms have the ability to bind to E-selectin and to inhibit complement activation. We suggest that AGP glycoforms in PMN provide an endogenous feedback-inhibitory response to excessive inflammation. J. Leukoc. Biol. 78: 453-461; 2005.

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Section: Characteristics Of Pmn Agpmentioning

confidence: 92%

Section: Characteristics Of Pmn Agpmentioning

confidence: 93%

Section: Methodsmentioning

confidence: 99%

Section: Cryoimmunogold Electron Microscopymentioning

confidence: 99%

Section: N-glycosidase F (Pngase F) Treatment and Monosaccharide Analmentioning

confidence: 99%

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Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Poland¹,

Vallejo²,

Niessen

et al. 2005

Journal of Leukocyte Biology

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Could the glycosylation analysis of seminal plasma clusterin become a novel male infertility biomarker?

Janiszewska¹,

Kratz²

2020

Molecular Reproduction Devel

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Male infertility is becoming a rapidly growing problem around the world, mainly in the highly developed countries. Seminal proteome composition seems to be one of the crucial factors of the proper course of fertilizationclusterin (CLU) is among the most important ones. CLU, as one of the crucial seminal plasma glycoproteins, plays a very important role in sperm capacitation and immune tolerance in the female reproductive tract. CLU is also known as a sensitive marker of oxidative stress. It has six N-glycosylation sites and also exhibits chaperone activity. An analysis of changes in the profile and degree of CLU glycosylation may shed some new light on the molecular mechanisms of the fertilization process and may be used as an additional diagnostic marker of male fertility. This study constitutes a review of the recently available literature concerning human seminal CLU, including changes in its glycosylation, analyzed in the context of human reproduction. K E Y W O R D S clusterin, male fertility, semen quality, seminal clusterin glycosylation

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Changes in glycosylation of human blood plasma chitotriosidase in patients with type 2 diabetes

et al. 2015

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Human blood plasma chitotriosidase (CHIT1) is a glycoprotein with chitinolytic activity with not fully elucidated biological function. Its increased level is observed in type 2 diabetes mellitus (T2DM) and is associated with development of diabetic complications. The CHIT1 glycosylation profile and degree is still poorly studied and never investigated in T2DM. Therefore the aim of the present study was to examine the association between glycosylation profile and degree and diabetes with accompanying nephropathy. In blood plasma of 28 patients with T2DM and 11 healthy subjects the CHIT1 concentration and specific activity were examined. The profile and degree of CHIT1 glycosylation were determined by lectin-ELISA using lectins specific to O-glycans (Jacalin, MPL, VVL) and sialo-specific SNA and MAA. We revealed that both concentration and specific activity of CHIT1 significantly increased in T2DM, especially in nephropathy with elevated albuminuria. The relative reactivities with lectins, except Jacalin, decreased progressively with T2DM occurrence and albuminuria progression. The most significant differences were observed between control vs. albuminuric group (Micro and Macro). It is also possible that the observed differences in immunoblotting pattern in molecular masses of CHIT1 bands between T2DM patients and healthy subjects may be caused by the differences in degree of CHIT1 glycosylation. The analysis of CHIT1 glycosylation status and the determination of CHIT1 concentration together with its enzymatic activity in blood plasma might constitute additional valuable diagnosis tools for the evaluation the T2DM patients with accompanying nephropathy. Extension of the lectin panel specific to O-glycans occurs useful for the further research using microarray formats, which are expected to accelerate “lectin-based glycan profiling” of glycoproteins.

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High level of α₁‐acid glycoprotein in human seminal plasma is associated with high branching and expression of Lewis^a groups on its glycans: Supporting evidence for a prostatic origin

Abstract: The results indicate that AGP in seminal fluid most likely originates from the prostate and that it is either alpha3- or alpha4-fucosylated.

Cited by 22 publications

References 33 publications

Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Could the glycosylation analysis of seminal plasma clusterin become a novel male infertility biomarker?

Changes in glycosylation of human blood plasma chitotriosidase in patients with type 2 diabetes

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High level of α1‐acid glycoprotein in human seminal plasma is associated with high branching and expression of Lewisa groups on its glycans: Supporting evidence for a prostatic origin

Abstract: The results indicate that AGP in seminal fluid most likely originates from the prostate and that it is either alpha3- or alpha4-fucosylated.

Cited by 22 publications

References 33 publications

Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Could the glycosylation analysis of seminal plasma clusterin become a novel male infertility biomarker?

Changes in glycosylation of human blood plasma chitotriosidase in patients with type 2 diabetes

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Product

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High level of α₁‐acid glycoprotein in human seminal plasma is associated with high branching and expression of Lewis^a groups on its glycans: Supporting evidence for a prostatic origin