α-Amylase is expressed in cotyledons of germinated Vigna mungo seeds and is responsible for the degradation of starch that is stored in the starch granule (SG). Immunocytochemical analysis of the cotyledon cells with anti–α-amylase antibody showed that α-amylase is transported to protein storage vacuole (PSV) and lytic vacuole (LV), which is converted from PSV by hydrolysis of storage proteins. To observe the insertion/degradation processes of SG into/in the inside of vacuoles, ultrastructural analyses of the cotyledon cells were conducted. The results revealed that SG is inserted into LV through autophagic function of LV and subsequently degraded by vacuolar α-amylase. The autophagy for SG was structurally similar to micropexophagy detected in yeast cells. In addition to the autophagic process for SG, autophagosome-mediated autophagy for cytoplasm and mitochondria was detected in the cotyledon cells. When the embryo axes were removed from seeds and the detached cotyledons were incubated, the autophagosome-mediated autophagy was observed, but the autophagic process for the degradation of SG was not detected, suggesting that these two autophagic processes were mediated by different cellular mechanisms. The two distinct autophagic processes were thought to be involved in the breakdown of SG and cell components in the cells of germinated cotyledon.
Skip Nav Destination
Article navigation
3 September 2001
Article|
August 27 2001
Cotyledon cells of Vigna mungo seedlings use at least two distinct autophagic machineries for degradation of starch granules and cellular components
Kiminori Toyooka,
Kiminori Toyooka
1Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, 192-0397 Japan
2Department of Infectious Diseases and Tropical Medicine, International Medical Center of Japan, Tokyo, 162-8655 Japan
Search for other works by this author on:
Takashi Okamoto,
Takashi Okamoto
1Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, 192-0397 Japan
Search for other works by this author on:
Takao Minamikawa
Takao Minamikawa
1Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, 192-0397 Japan
Search for other works by this author on:
Kiminori Toyooka
1Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, 192-0397 Japan
2Department of Infectious Diseases and Tropical Medicine, International Medical Center of Japan, Tokyo, 162-8655 Japan
Takashi Okamoto
1Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, 192-0397 Japan
Takao Minamikawa
1Department of Biological Sciences, Tokyo Metropolitan University, Tokyo, 192-0397 Japan
Address correspondence to Dr. Takashi Okamoto, Department of Biological Sciences, Tokyo Metropolitan University, Minami-osawa, Hachioji, Tokyo, 192-0397 Japan. Tel.: 81-426-77-2562. Fax: 81-426-77-2559. E-mail: [email protected]
*
Abbreviations used in this paper: KV, KDEL-tailed cysteine proteinase–accumulating vesicle; LED, low electron density; LV, lytic vacuole; PSV, protein storage vacuole; SG, starch granule, VB, vascular bundle.
Received:
May 21 2001
Revision Received:
July 05 2001
Accepted:
July 16 2001
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2001
J Cell Biol (2001) 154 (5): 973–982.
Article history
Received:
May 21 2001
Revision Received:
July 05 2001
Accepted:
July 16 2001
Citation
Kiminori Toyooka, Takashi Okamoto, Takao Minamikawa; Cotyledon cells of Vigna mungo seedlings use at least two distinct autophagic machineries for degradation of starch granules and cellular components . J Cell Biol 3 September 2001; 154 (5): 973–982. doi: https://doi.org/10.1083/jcb.200105096
Download citation file:
Sign in
Don't already have an account? Register
Client Account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your Institution
Sign in via your InstitutionEmail alerts
Advertisement
Advertisement