Overactive bladder (OAB) syndrome, characterised by urinary urgency, frequency, and nocturia can significantly impacts patients' quality of life. Current diagnosis is clinical, but complex cases often Show more
Overactive bladder (OAB) syndrome, characterised by urinary urgency, frequency, and nocturia can significantly impacts patients' quality of life. Current diagnosis is clinical, but complex cases often require invasive urodynamic studies (UDS), which are costly, subjective, and carry risks like discomfort and infection. Therefore, we hypothesise that urinary biomarkers could serve as noninvasive diagnostic tools for OAB. Establishing a reliable biomarker profile could ultimately lessen the reliance on invasive US, provided clinical validity is confirmed. Following PRISMA guidelines and registered under PROSPERO (ID: CRD420251026279), a comprehensive search across six major databases was conducted from their inception until September 2025, yielding 39 studies for qualitative analysis. This qualitative review identified several promising biomarkers for OAB diagnosis. Notably, NGF and BDNF consistently emerged as elevated in OAB patients and were responsive to treatment. Additionally, TNF-α, MIP-1β, Tie2, and CCL2 showed diagnostic potential, with TNF-α and MIP-1β particularly useful for differentiating OAB from interstitial cystitis/bladder pain syndrome (IC/BPS) and urinary tract infections (UTIs). However, limitations such as variability in measurement protocols and a lack of specificity for certain biomarkers (e.g. MMP-1, 8-OHdG) were noted. Urinary biomarkers offer a promising noninvasive approach to diagnosing OAB. Further validation of promising markers, particularly NGF, BDNF, TNF-α, MIP-1β, and CCL2, could lead to individualised therapies. While promising, the routine replacement of UDS remains an aspirational goal dependent on future large-scale validation. Show less
The spectrin superfamily (spectrin, alpha-actinin, utrophin and dystrophin) has in common a triple helical repeating unit of ~106 amino acid residues. In spectrin, alpha and beta chains contain multip Show more
The spectrin superfamily (spectrin, alpha-actinin, utrophin and dystrophin) has in common a triple helical repeating unit of ~106 amino acid residues. In spectrin, alpha and beta chains contain multiple copies of this repeat. beta-spectrin chains contain the majority of binding activities in spectrin and are essential for animal life. Canonical beta-spectrins have 17 repeats; beta-heavy spectrins have 30. Here, the repeats of five human beta-spectrins, plus beta-spectrins from several other vertebrates and invertebrates, have been analysed. Repeats 1, 2, 14 and 17 in canonical beta are highly conserved between invertebrates and vertebrates, and repeat 8 in some isoforms. This is consistent with conservation of critical functions, since repeats 1, 2 and 17 bind alpha-spectrin. Repeats 1 of beta-spectrins are not always detected by SMART or Pfam tools. A profile hidden Markov model of beta-spectrin repeat 1 detects alpha-actinins, but not utrophin or dystrophin. Novel examples of repeat 1 were detected in the spectraplakins MACF1, BPAG1 and plectin close to the actin-binding domain. Ankyrin binds to the C-terminal portion of repeat 14; the high conservation of this entire repeat may point to additional, undiscovered ligand-binding activities. This analysis indicates that the basic triple helical repeat pattern was adapted early in the evolution of the spectrin superfamily to encompass essential binding activities, which characterise individual repeats in proteins extant today. Show less