Volume 4, Issue 4, Pages (January 1998)

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Volume 4, Issue 4, Pages 289-294 (January 1998) Distribution and developmental changes of annexin V in rat pancreatic islets Reiko Miyoshi, Masaaki Tokuda, Makoto Ohnishi, Nobuhisa Uemura, Yuka A Hosokawa, Hitoshi Hosokawa, Koichi Kawanishi, Osamu Hatase, Toshihiko Ishida, Jiro Takahara Pathophysiology Volume 4, Issue 4, Pages 289-294 (January 1998) DOI: 10.1016/S0928-4680(97)10006-2

Fig. 1 Western blot analysis of pancreatic islets from 12 w.o. rats using anti-annexin V polyclonal antibody. In lanes a, b, c and d; 15, 30, 45 and 60 μg of homogenates of islets with buffer A, respectively, were applied on a 12.5% SDS-PAGE. Lane e represents a homogenate of a rat heart as a positive control (300 μg). Proteins were electrophoretically transferred onto a nitrocellulose membrane from the gel. The membrane was then incubated with anti-annexin V antibody. Molecular masses are given on the left in kDa. Pathophysiology 1998 4, 289-294DOI: (10.1016/S0928-4680(97)10006-2)

Fig. 2 Ca2+-dependent association of annexin V to membranes. Pancreatic islets from 12 w.o. rats were homogenized with buffer B (lanes c, d) or buffer C (lanes a, b) as described in Section 2. Following centrifugation, 30 μg of supernatants (SN) and pellets (P) were separated by SDS-PAGE, transferred to a nitrocellulose membrane, and the blot was probed with anti-annexin V antibody. Pathophysiology 1998 4, 289-294DOI: (10.1016/S0928-4680(97)10006-2)

Fig. 3 Distribution of annexin V-positive cells in adult pancreatic islets. Localization of annexin V, insulin and glucagon in rat pancreatic islets was analyzed using the respective antibodies as described in Section 2. All sections were adjacent, and were stained with non-immune rabbit IgG (A), anti-annexin V polyclonal antibody (B), anti-insulin polyclonal antibody (C), and anti-glucagon polyclonal antibody (D). Brown color indicates positive immunoreaction. Bars=50 μm. Pathophysiology 1998 4, 289-294DOI: (10.1016/S0928-4680(97)10006-2)

Fig. 4 Western blot analysis of annexin V in pancreatic islets during postnatal development. Lanes a, b, c, d and e indicate 3, 6, 9, 12 and 15 w.o. rats, respectively. Forty micrograms of 20 000×g supernatant per lane were separated by SDS-PAGE. Lane f represents purified bovine lung annexin V (6 μg). The blot was probed with anti-annexin V antibody. Pathophysiology 1998 4, 289-294DOI: (10.1016/S0928-4680(97)10006-2)

Fig. 5 Densitometric analysis of the change of annexin V in rat pancreatic islets. The density of immunoreacted bands of the homogenates of 3, 6, 9, 12 and 15 w.o. rats were analyzed. Values are expressed as mean±S.E.M. for five independent experiments. *P<0.05 vs. the corresponding values in 6 w.o. rats; **P<0.01 vs. the corresponding values in 3 w.o. rats. Pathophysiology 1998 4, 289-294DOI: (10.1016/S0928-4680(97)10006-2)

Fig. 6 Immunohistochemical detection of annexin V in rat pancreatic islets during postnatal development. One w.o. rat (A), 3 w.o. rat (B), 6 w.o. rat (C), 12 w.o. rat (D). Arrows represent islets of Langerhans. Bars=50 μm. Pathophysiology 1998 4, 289-294DOI: (10.1016/S0928-4680(97)10006-2)