Incorporation of heparin-binding proteins into preformed dextran sulfate-chitosan nanoparticles

ABSTRACT: Studies have been performed to identify the proteins present in canine seminal plasma (SP) and relate them to sperm quality as well as to discover molecular markers of reproductive tract diseases. There is evidence that heparin-binding proteins, zinc-binding proteins, and lactoferrin as well as the matrix metalloproteinase, superoxide dismutase, catalase, and glutathione peroxidase enzymes are associated with canine sperm quality. Other studies indicate that prolactin and enzymes like arginine esterase, acid phosphatase, and alkaline phosphatase could be successfully used as biomarkers of reproductive disorders. Thus, the present literature review aims to address aspects related to proteins of the canine SP, their influence on fertility, and their importance as biomarkers of reproductive disorders.

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The Tyrosine Sulfate-rich Domains of the LRR Proteins Fibromodulin and Osteoadherin Bind Motifs of Basic Clusters in a Variety of Heparin-binding Proteins, Including Bioactive Factors

Journal of Biological Chemistry ◽

10.1074/jbc.m109.047076 ◽

2009 ◽

Vol 284 (42) ◽

pp. 28543-28553 ◽

Cited By ~ 36

Author(s):

Viveka Tillgren ◽

Patrik Önnerfjord ◽

Lisbet Haglund ◽

Dick Heinegård

Keyword(s):

Binding Proteins ◽

Heparin Binding

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Application of a β-cyclodextrin sulfate-immobilized precolumn to selective on-line enrichment and separation of heparin-binding proteins by column-switching high-performance liquid chromatography

Journal of Chromatography A ◽

10.1016/s0021-9673(97)00088-5 ◽

1997 ◽

Vol 769 (2) ◽

pp. 209-214 ◽

Cited By ~ 5

Author(s):

Kimihiro Ishimura ◽

Kazuhiro Fukunaga ◽

Tetsumi Irie ◽

Kaneto Uekama ◽

Takafumi Ohta ◽

...

Keyword(s):

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

High Performance ◽

Binding Proteins ◽

Column Switching ◽

Heparin Binding ◽

On Line

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CD44 isoforms containing exon V3 are responsible for the presentation of heparin-binding growth factor.

The Journal of Cell Biology ◽

10.1083/jcb.128.4.687 ◽

1995 ◽

Vol 128 (4) ◽

pp. 687-698 ◽

Cited By ~ 269

Author(s):

K L Bennett ◽

D G Jackson ◽

J C Simon ◽

E Tanczos ◽

R Peach ◽

...

Keyword(s):

Endothelial Cells ◽

Growth Factors ◽

Growth Factor ◽

Binding Proteins ◽

Vascular Endothelial Cells ◽

Heparin Binding ◽

Binding Studies ◽

Cd44 Isoforms ◽

Cultured Endothelial Cells ◽

Alternatively Spliced

Glycosaminoglycan-modified isoforms of CD44 have been implicated in growth factor presentation at sites of inflammation. In the present study we show that COS cell transfectants expressing CD44 isoforms containing the alternatively spliced exon V3 are modified with heparan sulfate (HS). Binding studies with three HS-binding growth factors, basic-fibroblast growth factor (b-FGF), heparin binding-epidermal growth factor (HB-EGF), and amphiregulin, showed that the HS-modified CD44 isoforms are able to bind to b-FGF and HB-EGF, but not AR. b-FGF and HB-EGF binding to HS-modified CD44 was eliminated by pretreating the protein with heparitinase or by blocking with free heparin. HS-modified CD44 immunoprecipitated from keratinocytes, which express a CD44 isoform containing V3, also bound to b-FGF. We examined whether HS-modified CD44 isoforms were expressed by activated endothelial cells where they might present HS-binding growth factors to leukocytes during an inflammatory response. PCR and antibody-binding studies showed that activated cultured endothelial cells only express the CD44H isoform which does not contain any of the variably spliced exons including V3. Immunohistological studies with antibodies directed to CD44 extracellular domains encoded by the variably spliced exons showed that vascular endothelial cells in inflamed skin tissue sections do not express CD44 spliced variants. Keratinocytes, monocytes, and dendritic cells in the same specimens were found to express variably spliced CD44. 35SO4(-2)-labeling experiments demonstrated that activated cultured endothelial cells do not express detectable levels of chondroitin sulfate or HS-modified CD44. Our results suggest that one of the functions of CD44 isoforms expressing V3 is to bind and present a subset of HS-binding proteins. Furthermore, it is probable that HS-modified CD44 is involved in the presentation of HS-binding proteins by keratinocytes in inflamed skin. However, our data suggests that CD44 is not likely to be the proteoglycan principally involved in presenting HS-binding growth factors to leukocytes on the vascular cell wall.

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Heparin-binding proteins of canine seminal plasma

Theriogenology ◽

10.1016/j.theriogenology.2006.02.016 ◽

2006 ◽

Vol 66 (6-7) ◽

pp. 1606-1609 ◽

Cited By ~ 12

Author(s):

Fabiana Ferreira de Souza ◽

Maria Isabel Mello Martins ◽

Carlos Eurico dos Santos Fernandes ◽

Paulo Eduardo Martins Ribolla ◽

Maria Denise Lopes

Keyword(s):

Seminal Plasma ◽

Binding Proteins ◽

Heparin Binding

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SUPPRESSION EFFECT OF MAHKOTA DEWA (PHALERIA MACROCARPA) LEAF EXTRACT IN CHITOSAN NANOPARTICLES ON THE SMALL INTESTINE OF DEXTRAN SULFATE SODIUM-INDUCED MICE: FOCUS ON MITOSIS AND HYPERPLASIA

Asian Journal of Pharmaceutical and Clinical Research ◽

10.22159/ajpcr.2018.v11i6.24159 ◽

2018 ◽

Vol 11 (6) ◽

pp. 118

Author(s):

Kusmardi Kusmardi ◽

Arif Ramadhan Tamzir ◽

Santi Widiasari ◽

Ari Estuningtyas

Keyword(s):

Small Intestine ◽

Leaf Extract ◽

Dextran Sulfate ◽

Dextran Sulfate Sodium ◽

Chitosan Nanoparticles ◽

Negative Control ◽

Suppression Effect ◽

Significant Difference ◽

Phaleria Macrocarpa

Objective: The incidence of small intestine cancer (SIC) is rising despite available preventive measures. Kaempferol and quercetin are a potential chemopreventive agent for SIC, but in vivo findings are inconclusive. We aim to study the effects of kaempferol and quercetin on colitis-associated small intestine carcinogenesis in mice.Methods: Suppression effect was tested using mice divided into 6 groups of treatment, i.e.; normal (N) group, negative control (NC), leaf extract (medium dose [MD]) dose 12.5 and 25 mg/kg body weight (BW), leaf extract chitosan and nanoparticle of mahkota dewa (NPMD) dose 6.25 and 12.5 mg/kg BW. Dextran sulfate sodium induction of 1% w/v was administered through drinking water for 6 weeks of treatment. The suppression effect was observed histopathologically by counting the mitotic cells and hyperplasia cells of the crypt of small intestine with hematoxylin-eosin staining.Results: Mitosis cells mean of NC group was not significant difference either with MD 12.5 (p=0.394) or MD 6.5 (p=0.310). However, mitosis cell mean appears to be lower in the NPMD 12.5 (p=0.09) and NPMD 6.25 (p=0.05) groups than the NC group. There was a significant difference among the mean of hyperplasia NC group and MD and also NPMD group. Significant difference also can be showed between MD 12.5 and MD 25 (p=0.026), and between NPMD 6.25 and NPMD 12.5 (p=0.002), and between MD 12.5 and NPMD 12.5 (p=0.002).Conclusion: Our results demonstrate suppression of hyperplasia small intestine by either nanoparticle or extract of Phaleria macrocarpa extracts. The suppression of mitosis was showed by administration of nanoparticle.

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Heparin- and Zn2+-binding proteins from boar seminal plasma.

Acta Biochimica Polonica ◽

10.18388/abp.1999_4116 ◽

1999 ◽

Vol 46 (4) ◽

pp. 935-939 ◽

Cited By ~ 5

Author(s):

D Hołody ◽

J Strzezek

Keyword(s):

Amino Acid ◽

Affinity Chromatography ◽

Molecular Mass ◽

Seminal Plasma ◽

Binding Proteins ◽

Reproductive Tract ◽

Female Reproductive Tract ◽

Heparin Binding ◽

Sds Page ◽

Protein Components

Low molecular mass, heparin-binding proteins from seminal plasma play an important role in gametes interaction whereas plasmatic Zn2+-binding proteins stabilize chromatin and plasmalemma structures and protect spermatozoa in the female reproductive tract. By means of affinity chromatography the heparin- and Zn2+-binding proteins were isolated from boar seminal plasma and both preparations were analyzed by reverse HPLC. Most of the proteins bound to heparine and Zn2+-ions were classified as spermadhesins. Three fractions binding exclusively Zn2+ were isolated. They differ in amino-acid composition, content of glucosamine and content of protein components revealed by SDS/PAGE.

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