Lamellar bodies
In cell biology, lamellar bodies (otherwise known as lamellar granules, membrane-coating granules (MCGs), keratinosomes or Odland bodies) are secretory organelles found in type II alveolar cells in the lungs, and in keratinocytes in the skin. They are oblong structures, appearing about 300-400 nm in width and 100-150 nm in length in transmission electron microscopy images. Lamellar bodies in the alveoli of the lungs fuse with the cell membrane and release pulmonary surfactant into the extracellular space.[1][2]
Role in lungs
[edit]In alveolar cells the phosphatidylcholines (choline-based phospholipids) that are stored in the lamellar bodies serve as pulmonary surfactant after being released from the cell. In 1964, using transmission electron microscopy, which at that time was a relatively new tool for ultrastructural elucidation, John Balis identified the presence of lamellar bodies in type II alveolar cells, and further noted that upon their exocytotic migration to the alveolar surface, lamellar contents would uniformly unravel and spread along the circumference of the alveolus, thus lowering surface tension and similarly, the required alveolar inflation force.[3]
Role in epidermis
[edit]In the upper stratum spinosum and stratum granulosum layers of the epidermis, lamellar bodies are secreted from keratinocytes, resulting in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function. These bodies release components that are required for skin shedding (desquamation) in the uppermost epidermal layer, the stratum corneum.[4] These components include lipids (e.g. glucosylceramides), hydrolytic enzymes (e.g. proteases, acid phosphatases, glucosidases, lipases) and proteins (e.g. corneodesmosin).[5] Lamellar bodies have been observed to contain distinct aggregates of the secreted components glucosylceramide, cathepsin D, KLK7, KLK8 and corneodesmosin. Transportation of molecules via lamellar bodies is thought to prevent enzymes from interacting with their relevant substrates or inhibitors prior to secretion.[5]
Recent work suggests that lamellar bodies form a continuous membranous structure with the trans-Golgi network.
Lamellar body secretion and lipid structure is abnormal in the epidermis of patients with Netherton syndrome, a skin disorder characterised by chronic inflammation and universal pruritus (itch).
Deficient lipid membrane causes cold damage in patients of asteatotic eczema (also known as winter eczema).[6]
See also
[edit]References
[edit]- ^ Ishida-Yamamoto, Akemi; Kishibe, Mari (23 March 2011). "Involvement of corneodesmosome degradation and lamellar granule transportation in the desquamation process". Medical Molecular Morphology. 44 (1): 1–6. doi:10.1007/s00795-010-0513-4. PMID 21424930. S2CID 320940.
- ^ Tortora and Derrickson, Gerard J. and Bryan H. (2011). Principles of anatomy and physiology (13th ed.). Hoboken, N.J.: Wiley. p. 158. ISBN 978-0-470-64608-3.
- ^ Balis, J.U.; Conen, P.E. (1964). "The Role of Alveolar Inclusion Bodies in the Developing Lung". Lab Invest. 13: 1215–29. PMID 14212352.
- ^ Descargues, Pascal; Deraison, Céline; Bonnart, Chrystelle; Kreft, Maaike; Kishibe, Mari; Ishida-Yamamoto, Akemi; Elias, Peter; Barrandon, Yann; Zambruno, Giovanna; Sonnenberg, Arnoud; Hovnanian, Alain (26 December 2004). "Spink5-deficient mice mimic Netherton syndrome through degradation of desmoglein 1 by epidermal protease hyperactivity". Nature Genetics. 37 (1): 56–65. doi:10.1038/ng1493. PMID 15619623. S2CID 11404025.
- ^ a b Ishida-Yamamoto, Akemi; Simon, Michel; Kishibe, Mari; Miyauchi, Yuki; Takahashi, Hidetoshi; Yoshida, Shigetaka; O'Brien, Timothy J.; Serre, Guy; Iizuka, Hajime (May 2004). "Epidermal Lamellar Granules Transport Different Cargoes as Distinct Aggregates". Journal of Investigative Dermatology. 122 (5): 1137–1144. doi:10.1111/j.0022-202x.2004.22515.x. PMID 15140216.
- ^ Fartasch, Manigé; Williams, Mary L.; Elias, Peter M. (1 July 1999). "Altered Lamellar Body Secretion and Stratum Corneum Membrane Structure in Netherton Syndrome". Archives of Dermatology. 135 (7): 823–832. doi:10.1001/archderm.135.7.823. PMID 10411158.