Localization of Epidermal Hyaluronic Acid Using the Hyaluronate Binding Region of Cartilage Proteoglycan as a Specific Probe

Tammi, Raija; Ripellino, James A.; Margolis, Richard U.; Tammi, Markku

doi:10.1111/1523-1747.ep12456530

Cited by 202 publications

(144 citation statements)

References 7 publications

Supporting

Mentioning

122

Contrasting

Unclassified

Order By: Relevance

“…Recently, Tammi and co-workers have shown that hyaluronate is present between the epithelial cells in the lower layers of the epidermis (18,19). In the present study, we have confirmed this observation and extended it to include a variety of other stratified epithelia.…”

Section: Discussionsupporting

confidence: 87%

The hyaluronate receptor is preferentially expressed on proliferating epithelial cells.

Alho

Underhill

1989

The Journal of Cell Biology

203

View full text Add to dashboard Cite

Abstract. In the present study, we have examined the distribution of the hyaluronate receptor as well as hyaluronate itself in a variety of adult tissues. The hyaluronate receptor was localized with a monoclonal antibody, termed K-3, while hyaluronate was localized using proteolytic fragments of cartilage proteoglycan. Staining with the K-3 monoclonal antibody revealed that the hyaluronate receptor was present in a variety of epithelia including the skin, cheek, tongue, esophagus, vagina, intestines, oviduct, and bladder. However, it was notably absent from epithelial cells of the cornea and stomach as well as from endothelial cells of blood vessels. When present, the hyaluronate receptor was preferentially located in regions of active cell growth, such as in the basal layers of stratified epithelium and at the base of the crypts of Lieberkuhn in intestinal epithelium. A similar phenomenon was observed in cultured 3T3 cells. Cultures of 3T3 cells that were actively proliferating were found to have greater amounts of the receptor than their nonproliferating counterparts. When the various tissues were examined for hyaluronate, it was found to have a widespread distribution, being present in most of the basement membranes and between the cells in stratified epithelium. Indeed, in many cases, the distribution of hyaluronate closely paralleled that of the hyaluronate receptor. These results suggest that the interaction between hyaluronate and its receptor is involved in cell-tosubstratum adhesion.

show abstract

Section: Discussionsupporting

confidence: 87%

The hyaluronate receptor is preferentially expressed on proliferating epithelial cells.

Alho

Underhill

1989

The Journal of Cell Biology

203

View full text Add to dashboard Cite

show abstract

“…In accordance with previous studies [9,44,29], type III collagen and hyaluronic acid stained intensely in the normal subpapillary connective tissue surrounding the haemangidmas and in the connective tissue matrix between the capillary loops. In contrast to this, staining for type III collagen was very weak in the thickened vascular wall of the haemangioma capillaries; in these areas there were also ultrastructurally only a few scattered collagen fibrils with a periodicity of 67 nm.…”

Section: Discussionsupporting

confidence: 92%

Increase in types IV and VI collagen in cherry haemangiomas

Tamm

Jungkunz

et al. 1992

Arch Dermatol Res

View full text Add to dashboard Cite

Summary. The capillaries in cherry haemangiomas show perivascular hyalinized sheaths. In order to clarify the nature of this sheath material, the extracellular matrix of cherry haemangiomas from 20 normal volunteers (age range 30-64 years) was investigated using immunohistochemical and electronmicroscopical methods. Antibodies against collagen types III, IV and VI and laminin were used. Hyaluronic acid was visualized using the hyaluronic acid binding region of the cartilage proteoglycan as ligand. Electronmicroscopically, the sheaths contained multilaminated basement membrane-like material, collagen fibres 20-25 nm thick with a periodicity of 67 nm and broadbanded aggregates with a periodicity of 100 nm (zebra bodies or fibrous long-spacing fibres). Immunohistochemically, type IV collagen was stained throughout the whole sheath material. Staining for laminin was more confined to the endothelial side of the sheath. Intense staining for type III collagen and hyaluronic acid was found in the connective tissue of the subpapillary layer and between the cherry haemangioma capillaries. Much weaker staining for type III coUagen and no staining for hyaluronic acid were found invariably in an area 4-10 [tm thick directly around the capillaries. Both sheath material and intercapillary connective tissue of the haemangiomas showed pronounced staining for collagen type VL Immunogold staining revealed that type VI collagen was localized to microfihrils 5-6 nm thick and to the broad-banded aggregates with 100 nm periodicity. These findings further underline the assumption that the broad-banded aggregates consist of type VI collagen.

show abstract

“…HABP is a complex of aggrecan and link protein, and is derived from bovine cartilage. [35][36][37] In our study, using this specific probe, the surfaces of the tendons with more HA (Groups 0.50:0.25, 0.50:1.00, 1.00:0.25, 1.00:1.00, and 2.00:1.00) were smoother and had lower gliding resistance after 1000 cycles compared to the groups with less HA retained on the surface after 1000 cycles.…”

Section: Discussionmentioning

confidence: 60%

Optimization of surface modifications of extrasynovial tendon to improve its gliding ability in a canine model in vitro

et al. 2006

View full text Add to dashboard Cite

Previous studies have shown that the carboxyl groups in hyaluronic acid (HA) could be activated by 1-ethy 1-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDC)/N-hydroxysuccinimide (NHS) to form intermediate O-acylisoureas, which can chemically bind to exposed amino groups on the tendon surface, leading to improved gliding ability. However, the optimal ratio and concentrations of the components in this chemical mixture were not investigated. The purpose of this study was to optimize the constituents of this tissue engineering approach to tendon surface modification, to reduce friction and improve durability. Peroneus longus (PL) tendons (n ¼ 40) were harvested from adult mongrel dogs along with the A2 pulley obtained from the ipsilateral hind paw. After the gliding resistance of the normal PL tendon was measured, the tendons were treated under varying concentrations of HA (0.5, 1, and 2%) and EDC/NHS (0.05, 0.25, and 1%) mixed with a 10% gelatin. Tendon friction was measured for 1000 cycles of simulated flexion/extension motion. Following testing, the residual HA on the tendon surface was evaluated by immunohistochemisty. The gliding resistance of the untreated PL tendons had a mean value of 0.087 AE 0.021 N. After surface treatment, there was no significant difference in friction due to HA concentration alone, but the concentration of EDC/NHS and the interaction between HA concentration and EDC/NHS concentration had a significant effect on friction. Regardless of HA concentration, the friction after 1000 cycles was significantly decreased in preparations which included a 1% concentration of EDC/ NHS. The tendons with lower gliding resistance presented a smoother surface on light microscopy and maintained more residual HA on the tendon surface. By varying the relative concentrations of HA, EDC, and NHS it is possible to optimize the effect of surface treatment on friction and durability in a canine extrasynovial tendon in vitro. ß

show abstract

Localization of Epidermal Hyaluronic Acid Using the Hyaluronate Binding Region of Cartilage Proteoglycan as a Specific Probe

Cited by 202 publications

References 7 publications

The hyaluronate receptor is preferentially expressed on proliferating epithelial cells.

The hyaluronate receptor is preferentially expressed on proliferating epithelial cells.

Increase in types IV and VI collagen in cherry haemangiomas

Optimization of surface modifications of extrasynovial tendon to improve its gliding ability in a canine model in vitro

Contact Info

Product

Resources

About