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 HYBID (alias KIAA1199/CEMIP) and hyaluronan synthase coordinately regulate hyaluronan metabolism in histamine-stimulated skin fibroblasts

2020 ◽  
Vol 295 (8) ◽  
pp. 2483-2494
Author(s):  
Hiroyuki Yoshida ◽  
Mika Aoki ◽  
Aya Komiya ◽  
Yoko Endo ◽  
Keigo Kawabata ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Fold Increase ◽  
Histamine Receptor ◽  
Skin Fibroblasts ◽  
Dependent Manner ◽  
Skin Damage ◽  
Photoaged Skin ◽  
Molecular Sizes ◽  
Ha Synthase ◽  
Hyaluronan Binding

The immune-regulatory compound histamine is involved in the metabolism of the essential skin component hyaluronan (HA). We previously reported that histamine up-regulates the expression of HYBID (hyaluronan-binding protein involved in hyaluronan depolymerization, also called CEMIP or KIAA1199), which plays a key role in HA degradation. However, no information is available about histamine's effects on HA synthase (HAS) expression, the molecular sizes of HA species produced, and histamine receptors and their signaling pathways in skin fibroblasts. Moreover, histamine's effects on photoaged skin remain elusive. Here, we show that histamine increases HA degradation by up-regulating HYBID and down-regulating HAS2 in human skin fibroblasts in a dose- and time-dependent manner and thereby decreases the total amounts and sizes of newly produced HA. Histamine H1 blocker abrogated the histamine effects on HYBID up-regulation, HAS2 suppression, and HA degradation. Histamine H1 agonist exhibited effects on HA levels, composition, and breakdown similar to those of histamine. Of note, blockade of protein kinase Cδ or PI3K–Akt signaling abolished histamine-mediated HYBID stimulation and HAS2 suppression, respectively. Immunohistochemical experiments revealed a significant ∼2-fold increase in tryptase-positive mast cells in photoaged skin, where HYBID and HAS2 expression levels were increased and decreased, respectively, compared with photoprotected skin. These results indicate that histamine controls HA metabolism by up-regulating HYBID and down-regulating HAS2 via distinct signaling pathways downstream of histamine receptor H1. They further suggest that histamine may contribute to photoaged skin damage by skewing HA metabolism toward degradation.

scholarly journals Role of glycine 221 in catalytic activity of hyaluronan-binding protein 2

2017 ◽  
Vol 292 (15) ◽  
pp. 6381-6388 ◽  
Author(s):  
Fabian Stavenuiter ◽  
Eduard H. T. M. Ebberink ◽  
Koen Mertens ◽  
Alexander B. Meijer
Keyword(s):  
Catalytic Activity ◽  
Binding Protein ◽  
Hyaluronan Binding

scholarly journals Secreted Factors from Keloid Keratinocytes Modulate Collagen Deposition by Fibroblasts from Normal and Fibrotic Tissue: A Pilot Study

Biomedicines ◽  
2020 ◽  
Vol 8 (7) ◽  
pp. 200
Author(s):  
Mansour A. Alghamdi ◽  
Laith N. AL-Eitan ◽  
Andrew Stevenson ◽  
Nutan Chaudhari ◽  
Nicole Hortin ◽  
...  
Keyword(s):  
Elective Surgery ◽  
Normal Skin ◽  
Skin Fibroblasts ◽  
Collagen Production ◽  
Skin Cells ◽  
Secreted Factors ◽  
Primary Fibroblasts ◽  
Keloid Fibroblasts

Interactions between keratinocytes and fibroblasts in the skin layers are crucial in normal tissue development, wound healing, and scarring. This study has investigated the role of keloid keratinocytes in regulating collagen production by primary fibroblasts in vitro. Keloid cells were obtained from removed patients’ tissue whereas normal skin cells were discarded tissue obtained from elective surgery procedures. Fibroblasts and keratinocytes were isolated, cultured, and a transwell co-culture system were used to investigate the effect of keratinocytes on collagen production using a ‘scar-in-a-jar’ model. Keloid fibroblasts produced significantly more collagen than normal skin fibroblasts in monoculture at the RNA, secreted protein, and stable fibrillar protein level. When keloid keratinocytes were added to normal skin fibroblasts, expression of collagen was significantly upregulated in most samples, but when added to keloid fibroblasts, collagen I production was significantly reduced. Interestingly, keloid keratinocytes appear to decrease collagen production by keloid fibroblasts. This suggests that signaling in both keratinocytes and fibroblasts is disrupted in keloid pathology.

The role of hyaluronan-binding protein in assembly of pericellular matrices

1992 ◽  
Vol 193 (2) ◽  
pp. 145-151 ◽  
Author(s):  
Qin Yu ◽  
Shib D. Banerjee ◽  
Bryan P. Toole
Keyword(s):  
Binding Protein ◽  
Hyaluronan Binding

scholarly journals Prognostic and Functional Role of Hyaluronan-binding Protein 1 (HABP1) in Pancreatic Ductal Adenocarcinoma

2020 ◽  
Author(s):  
Yasuhiro Adachi ◽  
Takuya Oba ◽  
Takao Amaike ◽  
Yuzan Kudo ◽  
Shiro Kohi ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Pancreatic Ductal Adenocarcinoma ◽  
Colony Formation ◽  
Functional Role ◽  
Binding Protein ◽  
Ductal Adenocarcinoma ◽  
Rank Test ◽  
And Migration ◽  
Hyaluronan Binding

Abstract Background: Hyaluronan-binding protein 1 (HABP1) is one of molecules that binds to hyaluronan and is involved in a variety of cellular processes including cell proliferation and migration. HABP1 has related to the progression of various cancers however there are few reports on the expression and function of HABP1 in pancreatic ductal adenocarcinoma (PDAC). We examined the expression and functional role of HABP1 in PDAC.Methods: (1) Immunohistochemical analysis of HABP1 protein was done in archival tissues from 105 PDAC patients. (2) We examined the functional effect of HABP1 on proliferation, colony formation, and migration in PDAC cells by knockdown of HABP1. Results: (1) HABP1 was overexpressed in 49(46.2%) of 106 PDAC patients. Overall survival was significantly shorter in patients with high HABP1 expression (median survival time of 12.8 months) than in those with low HABP1 expression (28.5 months) (log-rank test; p = 0.004). (2) Knockdown of HABP1 expression in PDAC cells resulted in decreased cell proliferation, colony formation and migration ability. Conclusion: HABP1 may serve as a prognosis factor in PDAC and could be a new therapeutic target.

Role of the LIM domain binding protein LDB1 and the LIM only factor LMO4 in SHH subgroup medulloblastoma

2014 ◽  
Vol 226 (03) ◽  
Author(s):  
S Hutter ◽  
PA Northcott ◽  
M Kool ◽  
SM Pfister ◽  
D Kawauchi ◽  
...  
Keyword(s):  
Binding Protein ◽  
Lim Domain
Sign in / Sign up

Export Citation Format

Share Document