Shedding light on structure, function and regulation of human sirtuins: a comprehensive review.
Level 5 - mechanism / opinion, no new human data
Narrative review synthesizing mechanistic and structural literature without original human experimental data
PubMed 36597461 · doi:10.1007/s13205-022-03455-1
What was done
A narrative literature review summarizing the structural characteristics, enzymatic activities, subcellular localizations, physiological functions, and natural/synthetic modulators (such as resveratrol) of the seven human sirtuin proteins (SIRT1–SIRT7).
What was found
The abstract reports qualitative mechanistic descriptions without quantitative numerical findings. SIRT1, SIRT6, and SIRT7 are localized in the nucleus; SIRT3, SIRT4, and SIRT5 in the mitochondria; and SIRT2 in the cytoplasm. Sirtuins contain N-terminal, C-terminal, and zinc-binding domains and act as NAD+-dependent deacylases (deacetylase, demalonylase, depalmitoylase, demyristoylase, desuccinylase) or mono-ADP-ribosyltransferases. Functionally, they modulate lipid and glucose homeostasis, insulin sensitivity, DNA repair, inflammation, neurogenesis, aging, and tumorigenesis in cancers including non-small cell lung and colorectal cancer.
Why it matters
Synthesizes current knowledge on sirtuin structure and regulation, framing these enzymes as potential molecular targets for metabolic diseases, cancer, and aging.
Limits
As a narrative review, it lacks a systematic search protocol, meta-analytic pooling, and risk-of-bias assessment. It presents no new empirical or clinical data, and the abstract reports no quantitative metrics or human trial results.
Cited by
- supports Sirtuins are NAD-dependent enzymes that remove acetyl, acyl, or succinyl modifications from lysine residues on proteins to regulate enzymes and mediate gene silencing.