2015
DOI: 10.1038/jid.2015.299
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Hyaluronidase-1 Is Mainly Functional in the Upper Granular Layer, Close to the Epidermal Barrier

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Cited by 11 publications
(17 citation statements)
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“…The low levels of Hyal1 mRNA and protein in the organotypic REK cultures, and appearance of the HYAL1 protein late in maturation, are in line with its strict location in the granular layer, where it has been suggested to act as a gatekeeper, restricting high‐molecular‐mass hyaluronan entering the stratum corneum …”
Section: Discussionmentioning
confidence: 63%
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“…The low levels of Hyal1 mRNA and protein in the organotypic REK cultures, and appearance of the HYAL1 protein late in maturation, are in line with its strict location in the granular layer, where it has been suggested to act as a gatekeeper, restricting high‐molecular‐mass hyaluronan entering the stratum corneum …”
Section: Discussionmentioning
confidence: 63%
“…The hyaluronidases (HYAL) 1 and 2 are expressed in the epidermis . HYAL1 probably degrades hyaluronan in the granular cells, whereas the role of HYAL2 is poorly understood. There are no reports concerning the epidermal expression of KIAA1199 (CEMIP), which is involved in hyaluronan degradation by fibroblasts .…”
mentioning
confidence: 99%
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“…Our attempts to ultrastructurally localize HA using HABP failed to reveal this GAG either in the extracellular spaces of SC or at the surface of native and delipidated corneocytes (data not shown). HA is mostly processed by hyaluronidase 1 during the transition between SG and SC but is not completely degraded. In fact, Sakai et al .…”
Section: Discussionmentioning
confidence: 99%
“…[12] Various types of hyaluronidases exist in nature, HYAL1 being the predominant one in the ECM, expressed in keratinocytes and fibroblasts of human skin. [13] HYAL1 is involved in biological processes such as angiogenesis [14] and skin photo-ageing. [15] We have previously designed HA-based micelles and vesicles resulting from the controlled self-assembly of amphiphilic copolymers.…”
mentioning
confidence: 99%