The specific localization of seminolipid molecular species on mouse testis during testicular maturation revealed by imaging mass spectrometry.

نویسندگان

  • Naoko Goto-Inoue
  • Takahiro Hayasaka
  • Nobuhiro Zaima
  • Mitsutoshi Setou
چکیده

More than 90% of the glycolipid in mammalian testis consists of a unique sulfated glyceroglycolipid called seminolipid. The galactosylation of the molecule is catalyzed by UDP-galactose:ceramide galactosyltransferase (CGT). Disruption of the CGT gene in mice results in male infertility due to the arrest of spermatogenesis, indicating that seminolipid plays an important role in reproductive function. Seminolipid molecules can be assigned to different molecular species based on the fatty acid composition. In this report, we investigated the localizations of the molecular species of seminolipid by imaging mass spectrometry and demonstrated that major molecule (C16:0-alkyl-C16:0-acyl) was expressed throughout the tubules: some (C16:0-alkyl-C14:0-acyl and C14:0-alkyl-C16:0-acyl) were predominantly expressed in spermatocytes and the other (C17:0-alkyl-C16:0-acyl) was specifically expressed in spermatids and spermatozoa. This is the first report to show the cell-specific localization of each molecular species of seminolipid during testicular maturation.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Interaction between basigin and monocarboxylate transporter 2 in the mouse testes and spermatozoa

Basigin is a member of the immunoglobulin superfamily and plays various important roles in biological events including spermatogenesis. To examine the basigin molecular variants during spermatogenesis and sperm maturation in the mouse, immunoprecipitated basigin samples from testis and epididymal spermatozoa were analyzed by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS). ...

متن کامل

Seminolipid and its precursor/degradative product, galactosylalkylacylglycerol, in the testis of saposin A- and prosaposin-deficient mice.

Sphingolipid activator proteins (saposins A, B, C, and D) are derived from a common precursor protein (prosaposin) and specifically activate in vivo degradation of glycolipids with short carbohydrate chains. A mouse model of prosaposin deficiency (prosaposin-/-) closely mimics the human disease with an elevation of multiple glycolipids. The recently developed saposin A-/- mice showed a chronic ...

متن کامل

Characterizing mouse male germ cell-specific actin capping protein α3 (CPα3): dynamic patterns of expression in testicular and epididymal sperm

Aim: To characterize mouse capping protein α3 (CPα3) during spermatogenesis and sperm maturation. Methods: We produced rat anti-CPα3 antiserum and examined the expression of CPα3 in various mouse tissues using Western blot analysis and the localization of CPα3 in testicular and epididymal sperm using immunohistochemical analyses. We also examined how the localization of CPα3 and β-actin (ACTB) ...

متن کامل

Examination of the immunohistochemical localization and gene expression by RT-PCR of the oxytocin receptor in diabetic and non-diabetic mouse testis

Objective(s): The aim of this study was to determine Oxytocin receptor (OTR) gene expression and localization in diabetic and non-diabetic mouse testes by RT-PCR and immunohistochemistry, respectively. Materials and Methods: In this study, 18 male BALB/c mice (8–12 weeks old) were used and divided into three groups: diabetic, sham, and control. Streptozotocin (STZ) was applied to the diabetic g...

متن کامل

Hook wire localization for testis sparing surgery.

OBJECTIVE To describe a novel technique for localizing small testicular mass during testicular-sparing surgery (TSS). METHODS AND RESULTS A 20-year-old man presented with bilateral testicular masses. Both alpha-fetoprotein (AFP) and beta-human chorionic gonadotropin (BHCG) levels were raised. Clinical and imaging studies revealed a 2.7 cm and 0.7 cm mass in the right and left testis, respecti...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Glycobiology

دوره 19 9  شماره 

صفحات  -

تاریخ انتشار 2009