scholarly journals Multi-functional, multicompartmental hyaluronan-binding protein 1 (HABP1/p32/gC1qR): implication in cancer progression and metastasis

Oncotarget ◽  
2018 ◽  
Vol 9 (12) ◽  
pp. 10784-10807 ◽  
Author(s):  
Paramita Saha ◽  
Kasturi Datta
Keyword(s):  
Cancer Progression ◽  
Binding Protein ◽  
Hyaluronan Binding

scholarly journals Overexpression of hyaluronan-binding protein 1 promotes the proliferation, migration, and invasion of malignant glioma

2020 ◽  
Vol 9 (1) ◽  
pp. 1-11
Author(s):  
Zijun Yang ◽  
Shu Song ◽  
Wenchao Yin ◽  
Xin Qian ◽  
Qiang Yu ◽  
...  
Keyword(s):  
Malignant Glioma ◽  
Binding Protein ◽  
Migration And Invasion ◽  
Hyaluronan Binding

scholarly journals Tetranectin Binds to the Kringle 1-4 Form of Angiostatin and Modifies Its Functional Activity

2004 ◽  
Vol 2004 (2) ◽  
pp. 73-78 ◽  
Author(s):  
Tirsit Mogues ◽  
Michael Etzerodt ◽  
Crystal Hall ◽  
Georg Engelich ◽  
Jonas H. Graversen ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Cancer Progression ◽  
Functional Activity ◽  
Binding Protein ◽  
Antiproliferative Activities

Tetranectin is a plasminogen kringle 4 domain-binding protein present in plasma and various tissue locations. Decreased plasma tetranectin or increased tetranectin in stroma of cancers correlates with cancer progression and adverse prognosis. A possible mechanism through which tetranectin could influence cancer progression is by altering activities of plasminogen or the plasminogen fragment, angiostatin. Tetranectin was found to bind to the kringle 1-4 form of angiostatin (ASTK1-4). In addition, tetranectin inhibited binding of plasminogen or ASTK1-4to extracellular matrix (ECM) deposited by endothelial cells. Finally, tetranectin partially counteracted the ability of ASTK1-4to inhibit proliferation of endothelial cells. This latter effect of tetranectin was specific for ASTK1-4since it did not counteract the antiproliferative activities of the kringle 1-3 form of angiostatin (ASTK1-3) or endostatin. These findings suggest that tetranectin may modulate angiogenesis through interactions with AST.

scholarly journals Deletion of Hybid (hyaluronan-binding protein involved in hyaluronan depolymerization) results in attenuation of osteoarthritis in mice

2021 ◽  
Author(s):  
Masahiro Momoeda ◽  
Susana de Vega ◽  
Haruka Kaneko ◽  
Chiho Yoshinaga ◽  
Masayuki Shimoda ◽  
...  
Keyword(s):  
Binding Protein ◽  
Hyaluronan Binding

scholarly journals Role of HYBID (Hyaluronan Binding Protein Involved in Hyaluronan Depolymerization), Alias KIAA1199/CEMIP, in Hyaluronan Degradation in Normal and Photoaged Skin

2019 ◽  
Vol 20 (22) ◽  
pp. 5804 ◽  
Author(s):  
Hiroyuki Yoshida ◽  
Yasunori Okada
Keyword(s):  
Binding Protein ◽  
Normal Skin ◽  
Collagen Fibers ◽  
Skin Fibroblasts ◽  
Photoaged Skin ◽  
Skin Photoaging ◽  
Skin Wrinkling ◽  
Initial Process ◽  
Hyaluronan Binding

Photoaged skin is characterized clinically by apparent manifestations such as wrinkles and sagging, and histologically by an accumulation of abnormal elastin and a severe loss of collagen fibers in the dermis. Quantitative and qualitative alterations in elastin and collagens are considered to be responsible for the formation of wrinkles and sagging. However, since the integrity of elastin and collagen fibers in the dermis is maintained by their interactions with hyaluronan (HA) and a proteoglycan network structure, HA degradation may be the initial process, prior to the breakdown of the fibrillary components, leading to wrinkles and sagging in photoaged skin. We have recently discovered a new HA-degrading mechanism mediated by HYBID (hyaluronan binding protein involved in hyaluronan depolymerization), alias KIAA1199/CEMIP, in human skin fibroblasts, and examined the implication of HYBID for skin photoaging. In this review, we give an overview of the characteristics of HYBID and its prospective roles in HA turnover in normal skin and excessive HA degradation in photoaged skin. In addition, we describe our data on the inhibition of HYBID activity and expression by plant extracts in skin fibroblasts; and propose novel strategies to prevent or improve photoaging symptoms, such as skin wrinkling, by inhibition of HYBID-mediated HA degradation.

scholarly journals Validation and evaluation of a common biomarker in human cancers sera protein detected by a monoclonal antibody UNIVmAb

2019 ◽  
Vol 12 (1) ◽  
Author(s):  
D. Manjunath ◽  
Sunil B. Kumaraswamy ◽  
Shashidhar Aladhi Venkatakrishniah ◽  
Hitesh Nidumanda Appaiah ◽  
Anil Thomas ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Western Blot ◽  
Anion Exchange ◽  
Binding Protein ◽  
Anion Exchange Column ◽  
Over Expression ◽  
Exchange Column ◽  
Human Cancers ◽  
Exclusion Chromatography ◽  
Hyaluronan Binding

Abstract Objective Management and diagnosis of multiple human cancers remains a challenge and search for a common biomarker is still debatable. In this manuscript we have evaluated the use of monoclonal antibody UNIVmAb, to detect the protein (H11) as a common biomarker for all cancers irrespective of the grade and origin. We have shown by both ELISA and Western Blot that the H11 protein, is a unique hyaluronan binding protein that has not been detected earlier. H11 protein was fractionated in an anion exchange column followed by cibacron blue gel exclusion chromatography. Hyaluronan binding H11 protein reacted with Monoclonal antibody UNIVmAb and b-HA inspite of b-Hyaluronan (biotinylated Hyaluronan) interaction and HA-Oligo (Hyaluronan oligosaccharides) competition from various grades of Human cancers sera. Results ELISA, Western blot and b-Hyaluronan interactions clearly showed an over-expression of UNIVmAb reacted H11 protein in all fifty cancer’s sera when compared with seventy normal sera. UNIVmAb reactive H11 protein can be used as a common biomarker. We believe, UNIVmAb detected H11 protein, is a unique hyaluronan binding protein, that can be used as a common biomarker for all cancers.

Segregation and expression analyses of hyaluronan-binding protein 2 (HABP2): insights from a large series of familial non-medullary thyroid cancers and literature review

2017 ◽  
Vol 86 (6) ◽  
pp. 837-844 ◽  
Author(s):  
Carla Colombo ◽  
Marina Muzza ◽  
Maria Carla Proverbio ◽  
Giulia Ercoli ◽  
Michela Perrino ◽  
...  
Keyword(s):  
Literature Review ◽  
Binding Protein ◽  
Large Series ◽  
Thyroid Cancers ◽  
Medullary Thyroid ◽  
Hyaluronan Binding
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