کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10755660 | 1050376 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Mouse liver lysosomes contain enzymatically active processed forms of Hyal-1
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کلمات کلیدی
RSAGPiDMABHYAL-1p-Dimethylaminobenzaldehyde - p-dimethylaminobenzaldehydeHyaluronic acid - اسید هیالورونیکTriton WR-1339 - تریتون WR-1339Fractionation - تقسیم بندیZymography - زیموگرافیendoplasmic reticulum - شبکه آندوپلاسمی Lysosome - لیزوزومLiver - کبدglycophosphatidylinositol - گلیکوفسفیدیدیلینواستیل
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
It has long been known that liver lysosomes contain an endoglycosidase activity able to degrade the high molecular mass glycosaminoglycan hyaluronic acid (HA). The identification and cloning of a hyaluronidase with an acidic pH optimum, Hyal-1, suggested it might be responsible for this activity. However, we previously reported that this hydrolase could only be detected in pre-lysosomal compartments of the mouse liver using a zymography technique that allows the detection of Hyal-1 activity after SDS-PAGE (“renatured protein zymography”). Present work reveals that the activity highlighted by this technique belongs to a precursor form of Hyal-1 and that the lysosomal HA endoglycosidase activity of the mouse liver is accounted for by a proteolytically processed form of Hyal-1 that can only be detected using “native protein zymography”. Indeed, the distribution of this form follows the distribution of β-galactosidase, a well-established lysosomal marker, after fractionation of the mouse liver in a linear sucrose density gradient. In addition, both activities shift toward the lower density region of the gradient when a specific decrease of the lysosomal density is induced by Triton WR-1339 injection. The fact that only native protein zymography but not renatured protein zymography is able to detect Hyal-1 activity in lysosomes points to a non-covalent association of Hyal-1 proteolytic fragments or the existence of closely linked partners supporting Hyal-1 enzymatic activity. The knockdown of Hyal-1 results in an 80% decrease of total acid hyaluronidase activity in the mouse liver, confirming that Hyal-1 is a key actor of HA catabolism in this organ.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 1155-1160
Journal: Biochemical and Biophysical Research Communications - Volume 446, Issue 4, 18 April 2014, Pages 1155-1160
نویسندگان
Marielle Boonen, Emeline Puissant, Florentine Gilis, Bruno Flamion, Michel Jadot,