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The underlying hydroxylation reaction is catalyzed by fatty acid 2-hydroxylase (FA2H). Deficiency in this enzyme causes a complicated hereditary spastic paraplegia, SPG35, which is associated with leukodystrophy. Mass spectrometry-based proteomics of purified myelin isolated from sciatic nerves of<jats:italic>Fa2h<\/jats:italic>-deficient (<jats:italic>Fa2h<\/jats:italic><jats:sup>\u2212\/\u2212<\/jats:sup>) mice revealed an increase in the concentration of the three proteins Cadm4, Mpp6 (Pals2), and protein band 4.1G (Epb41l2) in 17-month-old, but not in young (4 to 6-month-old),<jats:italic>Fa2h<\/jats:italic><jats:sup>\u2212\/\u2212<\/jats:sup>mice. These proteins are known to form a complex, together with the protein Lin7, in Schmidt-Lanterman incisures (SLIs). Accordingly, the number of SLIs was significantly increased in 17-month-old but not 4-month-old<jats:italic>Fa2h<\/jats:italic><jats:sup>\u2212\/\u2212<\/jats:sup>mice compared to age-matched wild-type mice. On the other hand, the relative increase in the SLI frequency was less pronounced than expected from Cadm4, Lin7, Mpp6 (Pals2), and band 4.1G (Epb41l2) protein levels. This suggests that the latter not only reflect the higher SLI frequency but that the concentration of the Cadm4 containing complex itself is increased in the SLIs or compact myelin of<jats:italic>Fa2h<\/jats:italic><jats:sup>\u2212\/\u2212<\/jats:sup>mice and may potentially play a role in the pathogenesis of the disease. The proteome data are available via ProteomeXchange with identifier PXD030244.<\/jats:p>","DOI":"10.1007\/s12035-022-02832-4","type":"journal-article","created":{"date-parts":[[2022,4,21]],"date-time":"2022-04-21T05:02:40Z","timestamp":1650517360000},"page":"3969-3979","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Age-Dependent Increase in Schmidt-Lanterman Incisures and a Cadm4-Associated Membrane Skeletal Complex in Fatty Acid 2-hydroxylase Deficient Mice: a Mouse Model of Spastic Paraplegia SPG35"],"prefix":"10.1007","volume":"59","author":[{"given":"Silvia","family":"Jordans","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert","family":"Hardt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ivonne","family":"Becker","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dominic","family":"Winter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lihua","family":"Wang-Eckhardt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1964-9064","authenticated-orcid":false,"given":"Matthias","family":"Eckhardt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2022,4,20]]},"reference":[{"key":"2832_CR1","doi-asserted-by":"publisher","first-page":"1095","DOI":"10.1083\/jcb.142.4.1095","volume":"142","author":"RJ Balice-Gordon","year":"1998","unstructured":"Balice-Gordon RJ, Bone LJ, Scherer SS (1998) Functional gap junctions in the schwann cell myelin sheath. 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